Ćirković-Veličković, Tanja

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Authority KeyName Variants
orcid::0000-0003-2559-5234
  • Ćirković-Veličković, Tanja (300)
Projects
Molecular properties and modifications of some respiratory and nutritional allergens FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics
Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200168 (University of Belgrade, Faculty of Chemistry)
Ispitivanje strukture i funkcije biološki važnih makromolekula u fiziološkim i patološkim stanjima Ghent University Global Campus, Belgian Special Research Fund BOF StG No. 01N01718.
Serbian Academy of Sciences and Arts Project F-26. Serbian Academy of Sciences and Arts GA No. F-26.
Swedish Research Council CAPSIDO – Developement of the assays for detection of SARS Cov-2 virus capsid proteins in biological fluids of COVID19 patients
King Gustaf V 80th Birthday Foundation Magnus Bergvall Foundation
Swedish Asthma and Allergy Associations Research Foundation Swedish Cancer and Allergy Foundation
Swedish Heart-Lung Foundation Stockholm County Council
Hesselman Foundation Structure-properties relationships of natural and synthetic molecules and their metal complexes
Allergens, antibodies, enzymes and small physiologically important molecules: design, structure, function and relevance Karolinska Institutet
COST Action [FA 1005] Rational design and synthesis of biologically active and coordination compounds and functional materials, relevant for (bio)nanotechnology
Swedish Association for Allergology Belgian Special Research Fund BOF StG No. 01N01718.
Center for Inflammatory Diseases Application of advanced oxidation processes and nanostructured oxide materials for the removal of pollutants from the environment, development and optimisation of instrumental techniques for efficiency monitoring
Serbian Academy of Sciences and Arts [GA No. F-26] The Hesselman Foundation.
The King Gustaf V 80th Birthday Foundation. The Konsul Th C Bergh Foundation.

Author's Bibliography

Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix

Khulal, Urmila; Stojadinović, Marija M.; Prodić, Ivana; Rajković, Andrea; Ćirković-Veličković, Tanja

(Elsevier, 2023)

TY  - JOUR
AU  - Khulal, Urmila
AU  - Stojadinović, Marija M.
AU  - Prodić, Ivana
AU  - Rajković, Andrea
AU  - Ćirković-Veličković, Tanja
PY  - 2023
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5765
AB  - The digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.
PB  - Elsevier
T2  - Food Chemistry
T1  - Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix
VL  - 405
SP  - 134981
DO  - 10.1016/j.foodchem.2022.134981
ER  - 
@article{
author = "Khulal, Urmila and Stojadinović, Marija M. and Prodić, Ivana and Rajković, Andrea and Ćirković-Veličković, Tanja",
year = "2023",
abstract = "The digestion stability of allergen pairs, tropomyosin, TM (fish and seafood allergen), and myosin light chain, MLC (chicken meat allergen) is compared among vertebrates and invertebrates in raw and cooked food matrix under standardized simulated in vitro gastrointestinal (GI) digestion. SDS-PAGE followed by multiple TM and MLC-specific antibodies in semidry WB revealed pepsin resistance of invertebrate TMs (abalone, oyster, shrimp) under diet-relevant conditions (raw, cooked). Vertebrate TMs (chicken, pork, beef) were less stable to digestion except that the raw chicken TM was observed pepsin resistant (not diet-relevant). Vertebrate (chicken) MLC was thermally stable. A new 28 kDa protein bound to anti-MLC antibody in cooked chicken and pork; could be the aggregates of MLC. Raw shrimp MLC showed pepsin resistance among invertebrates. A good correlation was observed between combined resistance of TM and MLC to GI digestion following the diet-relevant thermal treatment and reported protein allergenicity among vertebrates and invertebrates.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix",
volume = "405",
pages = "134981",
doi = "10.1016/j.foodchem.2022.134981"
}
Khulal, U., Stojadinović, M. M., Prodić, I., Rajković, A.,& Ćirković-Veličković, T.. (2023). Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry
Elsevier., 405, 134981.
https://doi.org/10.1016/j.foodchem.2022.134981
Khulal U, Stojadinović MM, Prodić I, Rajković A, Ćirković-Veličković T. Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix. in Food Chemistry. 2023;405:134981.
doi:10.1016/j.foodchem.2022.134981 .
Khulal, Urmila, Stojadinović, Marija M., Prodić, Ivana, Rajković, Andrea, Ćirković-Veličković, Tanja, "Comparative digestion of thermally treated vertebrates and invertebrates allergen pairs in real food matrix" in Food Chemistry, 405 (2023):134981,
https://doi.org/10.1016/j.foodchem.2022.134981 . .

Voltammetric immunoassay based on MWCNTs@Nd(OH)3-BSA-antibody platform for sensitive BSA detection

Đurđić, Slađana Z.; Ognjanović, Miloš; Krstić Ristivojević, Maja; Antić, Bratislav; Ćirković-Veličković, Tanja; Mutić, Jelena; Kónya, Zoltán; Stanković, Dalibor

(Springer, 2022)

TY  - JOUR
AU  - Đurđić, Slađana Z.
AU  - Ognjanović, Miloš
AU  - Krstić Ristivojević, Maja
AU  - Antić, Bratislav
AU  - Ćirković-Veličković, Tanja
AU  - Mutić, Jelena
AU  - Kónya, Zoltán
AU  - Stanković, Dalibor
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5670
AB  - An electrochemical approach is presented based on multiwall carbon nanotubes (MWCNTs) and neodymium(III) hydroxide (Nd(OH)3) nanoflakes for detection of bovine serum albumin (BSA). The materials were characterized morphologically (XRPD, SEM, and HR-TEM) and electrochemically (DPV, EIS). The MWCNTs@Nd(OH)3 composite was used as support for bovine serum albumin polyclonal antibody (anti-BSA). After the antibody immobilization on the electrochemical platform and antigen/antibody binding time (optimum 60 min), the proposed approach shows a linear voltammetric response toward BSA concentration in the range 0.066 to 6.010 ng mL−1 at maximum peak potential of 0.13 V (vs. Ag/AgCl). Limit of detection (LOD) and limit of quantification (LOQ) were 18 pg mL−1 and 61 pg mL−1, respectively. The precision of the method calculated as relative standard deviation (RSD) of five independent measurements was better 3%. The selectivity of the optimized method regarding structurally similar proteins (human serum albumin and human hemoglobin), ions (Na+, K+, Ca2+, and NO2−), or compounds (glucose, ascorbic acid, dopamine, uric acid, paracetamol, and glycine) was found to be satisfactory, with the current changes of less than 5% in the presence of up to 1 × 105 times higher concentrations (depending on the compound) of the listed potential interfering compounds. Practical applicability of immunosensor for BSA determination in cow whey sample, with recovery values in the range 97 to 103%, shows that the developed method has high potential for precise and accurate detection of BSA, as well as exceptional miniaturization possibilities for on-site and equipment-free sensing.
PB  - Springer
T2  - Microchimica Acta
T1  - Voltammetric immunoassay based on MWCNTs@Nd(OH)3-BSA-antibody platform for sensitive BSA detection
VL  - 189
IS  - 11
SP  - 422
DO  - 10.1007/s00604-022-05514-z
ER  - 
@article{
author = "Đurđić, Slađana Z. and Ognjanović, Miloš and Krstić Ristivojević, Maja and Antić, Bratislav and Ćirković-Veličković, Tanja and Mutić, Jelena and Kónya, Zoltán and Stanković, Dalibor",
year = "2022",
abstract = "An electrochemical approach is presented based on multiwall carbon nanotubes (MWCNTs) and neodymium(III) hydroxide (Nd(OH)3) nanoflakes for detection of bovine serum albumin (BSA). The materials were characterized morphologically (XRPD, SEM, and HR-TEM) and electrochemically (DPV, EIS). The MWCNTs@Nd(OH)3 composite was used as support for bovine serum albumin polyclonal antibody (anti-BSA). After the antibody immobilization on the electrochemical platform and antigen/antibody binding time (optimum 60 min), the proposed approach shows a linear voltammetric response toward BSA concentration in the range 0.066 to 6.010 ng mL−1 at maximum peak potential of 0.13 V (vs. Ag/AgCl). Limit of detection (LOD) and limit of quantification (LOQ) were 18 pg mL−1 and 61 pg mL−1, respectively. The precision of the method calculated as relative standard deviation (RSD) of five independent measurements was better 3%. The selectivity of the optimized method regarding structurally similar proteins (human serum albumin and human hemoglobin), ions (Na+, K+, Ca2+, and NO2−), or compounds (glucose, ascorbic acid, dopamine, uric acid, paracetamol, and glycine) was found to be satisfactory, with the current changes of less than 5% in the presence of up to 1 × 105 times higher concentrations (depending on the compound) of the listed potential interfering compounds. Practical applicability of immunosensor for BSA determination in cow whey sample, with recovery values in the range 97 to 103%, shows that the developed method has high potential for precise and accurate detection of BSA, as well as exceptional miniaturization possibilities for on-site and equipment-free sensing.",
publisher = "Springer",
journal = "Microchimica Acta",
title = "Voltammetric immunoassay based on MWCNTs@Nd(OH)3-BSA-antibody platform for sensitive BSA detection",
volume = "189",
number = "11",
pages = "422",
doi = "10.1007/s00604-022-05514-z"
}
Đurđić, S. Z., Ognjanović, M., Krstić Ristivojević, M., Antić, B., Ćirković-Veličković, T., Mutić, J., Kónya, Z.,& Stanković, D.. (2022). Voltammetric immunoassay based on MWCNTs@Nd(OH)3-BSA-antibody platform for sensitive BSA detection. in Microchimica Acta
Springer., 189(11), 422.
https://doi.org/10.1007/s00604-022-05514-z
Đurđić SZ, Ognjanović M, Krstić Ristivojević M, Antić B, Ćirković-Veličković T, Mutić J, Kónya Z, Stanković D. Voltammetric immunoassay based on MWCNTs@Nd(OH)3-BSA-antibody platform for sensitive BSA detection. in Microchimica Acta. 2022;189(11):422.
doi:10.1007/s00604-022-05514-z .
Đurđić, Slađana Z., Ognjanović, Miloš, Krstić Ristivojević, Maja, Antić, Bratislav, Ćirković-Veličković, Tanja, Mutić, Jelena, Kónya, Zoltán, Stanković, Dalibor, "Voltammetric immunoassay based on MWCNTs@Nd(OH)3-BSA-antibody platform for sensitive BSA detection" in Microchimica Acta, 189, no. 11 (2022):422,
https://doi.org/10.1007/s00604-022-05514-z . .
1

Supplementary material for: Đurđić, S., Ognjanović, M., Krstić Ristivojević, M., Antić, B., Ćirković Veličković, T., Mutić, J., Kónya, Z.,& Stanković, D.. (2022). Voltammetric immunoassay based on MWCNTs@Nd(OH)3-BSA-antibody platform for sensitive BSA detection. in Microchimica Acta Springer., 189(11), 422. https://doi.org/10.1007/s00604-022-05514-z

Ognjanović, Miloš; Krstić Ristivojević, Maja; Antić, Bratislav; Ćirković-Veličković, Tanja; Mutić, Jelena; Kónya, Zoltán; Stanković, Dalibor

(Springer, 2022)

TY  - DATA
AU  - Ognjanović, Miloš
AU  - Krstić Ristivojević, Maja
AU  - Antić, Bratislav
AU  - Ćirković-Veličković, Tanja
AU  - Mutić, Jelena
AU  - Kónya, Zoltán
AU  - Stanković, Dalibor
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5672
AB  - An electrochemical approach is presented based on multiwall carbon nanotubes (MWCNTs) and neodymium(III) hydroxide (Nd(OH)3) nanoflakes for detection of bovine serum albumin (BSA). The materials were characterized morphologically (XRPD, SEM, and HR-TEM) and electrochemically (DPV, EIS). The MWCNTs@Nd(OH)3 composite was used as support for bovine serum albumin polyclonal antibody (anti-BSA). After the antibody immobilization on the electrochemical platform and antigen/antibody binding time (optimum 60 min), the proposed approach shows a linear voltammetric response toward BSA concentration in the range 0.066 to 6.010 ng mL−1 at maximum peak potential of 0.13 V (vs. Ag/AgCl). Limit of detection (LOD) and limit of quantification (LOQ) were 18 pg mL−1 and 61 pg mL−1, respectively. The precision of the method calculated as relative standard deviation (RSD) of five independent measurements was better 3%. The selectivity of the optimized method regarding structurally similar proteins (human serum albumin and human hemoglobin), ions (Na+, K+, Ca2+, and NO2−), or compounds (glucose, ascorbic acid, dopamine, uric acid, paracetamol, and glycine) was found to be satisfactory, with the current changes of less than 5% in the presence of up to 1 × 105 times higher concentrations (depending on the compound) of the listed potential interfering compounds. Practical applicability of immunosensor for BSA determination in cow whey sample, with recovery values in the range 97 to 103%, shows that the developed method has high potential for precise and accurate detection of BSA, as well as exceptional miniaturization possibilities for on-site and equipment-free sensing.
PB  - Springer
T2  - Microchimica Acta
T1  - Supplementary material for: Đurđić, S., Ognjanović, M., Krstić Ristivojević, M., Antić, B., Ćirković Veličković, T., Mutić, J., Kónya, Z.,& Stanković, D.. (2022). Voltammetric immunoassay based on MWCNTs@Nd(OH)3-BSA-antibody platform for sensitive BSA detection. in Microchimica Acta Springer., 189(11), 422. https://doi.org/10.1007/s00604-022-05514-z
VL  - 189
IS  - 11
SP  - 422
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5672
ER  - 
@misc{
author = "Ognjanović, Miloš and Krstić Ristivojević, Maja and Antić, Bratislav and Ćirković-Veličković, Tanja and Mutić, Jelena and Kónya, Zoltán and Stanković, Dalibor",
year = "2022",
abstract = "An electrochemical approach is presented based on multiwall carbon nanotubes (MWCNTs) and neodymium(III) hydroxide (Nd(OH)3) nanoflakes for detection of bovine serum albumin (BSA). The materials were characterized morphologically (XRPD, SEM, and HR-TEM) and electrochemically (DPV, EIS). The MWCNTs@Nd(OH)3 composite was used as support for bovine serum albumin polyclonal antibody (anti-BSA). After the antibody immobilization on the electrochemical platform and antigen/antibody binding time (optimum 60 min), the proposed approach shows a linear voltammetric response toward BSA concentration in the range 0.066 to 6.010 ng mL−1 at maximum peak potential of 0.13 V (vs. Ag/AgCl). Limit of detection (LOD) and limit of quantification (LOQ) were 18 pg mL−1 and 61 pg mL−1, respectively. The precision of the method calculated as relative standard deviation (RSD) of five independent measurements was better 3%. The selectivity of the optimized method regarding structurally similar proteins (human serum albumin and human hemoglobin), ions (Na+, K+, Ca2+, and NO2−), or compounds (glucose, ascorbic acid, dopamine, uric acid, paracetamol, and glycine) was found to be satisfactory, with the current changes of less than 5% in the presence of up to 1 × 105 times higher concentrations (depending on the compound) of the listed potential interfering compounds. Practical applicability of immunosensor for BSA determination in cow whey sample, with recovery values in the range 97 to 103%, shows that the developed method has high potential for precise and accurate detection of BSA, as well as exceptional miniaturization possibilities for on-site and equipment-free sensing.",
publisher = "Springer",
journal = "Microchimica Acta",
title = "Supplementary material for: Đurđić, S., Ognjanović, M., Krstić Ristivojević, M., Antić, B., Ćirković Veličković, T., Mutić, J., Kónya, Z.,& Stanković, D.. (2022). Voltammetric immunoassay based on MWCNTs@Nd(OH)3-BSA-antibody platform for sensitive BSA detection. in Microchimica Acta Springer., 189(11), 422. https://doi.org/10.1007/s00604-022-05514-z",
volume = "189",
number = "11",
pages = "422",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5672"
}
Ognjanović, M., Krstić Ristivojević, M., Antić, B., Ćirković-Veličković, T., Mutić, J., Kónya, Z.,& Stanković, D.. (2022). Supplementary material for: Đurđić, S., Ognjanović, M., Krstić Ristivojević, M., Antić, B., Ćirković Veličković, T., Mutić, J., Kónya, Z.,& Stanković, D.. (2022). Voltammetric immunoassay based on MWCNTs@Nd(OH)3-BSA-antibody platform for sensitive BSA detection. in Microchimica Acta Springer., 189(11), 422. https://doi.org/10.1007/s00604-022-05514-z. in Microchimica Acta
Springer., 189(11), 422.
https://hdl.handle.net/21.15107/rcub_cherry_5672
Ognjanović M, Krstić Ristivojević M, Antić B, Ćirković-Veličković T, Mutić J, Kónya Z, Stanković D. Supplementary material for: Đurđić, S., Ognjanović, M., Krstić Ristivojević, M., Antić, B., Ćirković Veličković, T., Mutić, J., Kónya, Z.,& Stanković, D.. (2022). Voltammetric immunoassay based on MWCNTs@Nd(OH)3-BSA-antibody platform for sensitive BSA detection. in Microchimica Acta Springer., 189(11), 422. https://doi.org/10.1007/s00604-022-05514-z. in Microchimica Acta. 2022;189(11):422.
https://hdl.handle.net/21.15107/rcub_cherry_5672 .
Ognjanović, Miloš, Krstić Ristivojević, Maja, Antić, Bratislav, Ćirković-Veličković, Tanja, Mutić, Jelena, Kónya, Zoltán, Stanković, Dalibor, "Supplementary material for: Đurđić, S., Ognjanović, M., Krstić Ristivojević, M., Antić, B., Ćirković Veličković, T., Mutić, J., Kónya, Z.,& Stanković, D.. (2022). Voltammetric immunoassay based on MWCNTs@Nd(OH)3-BSA-antibody platform for sensitive BSA detection. in Microchimica Acta Springer., 189(11), 422. https://doi.org/10.1007/s00604-022-05514-z" in Microchimica Acta, 189, no. 11 (2022):422,
https://hdl.handle.net/21.15107/rcub_cherry_5672 .

Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating

Radomirović, Mirjana Ž.; Minić, Simeon L.; Stanić-Vučinić, Dragana; Nikolić, Milan; Van Haute, Sam; Rajković, Andreja; Ćirković-Veličković, Tanja

(Elsevier, 2022)

TY  - JOUR
AU  - Radomirović, Mirjana Ž.
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Van Haute, Sam
AU  - Rajković, Andreja
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4863
AB  - β-lactoglobulin (BLG) is a major whey protein with numerous techno-functional properties desirable for the food industry. Phycocyanobilin (PCB), a bioactive pigment of Arthrospira platensis with health-promoting effects, covalently binds to BLG at physiological pH. This study investigated the effects of this covalent modification on BLG functional properties. The BLG–PCB adduct possesses enhanced antioxidant properties, and bound PCB protects BLG against free radical-induced oxidation. Despite the similar thermal stabilities of BLG and BLG–PCB, BLG–PCB is less susceptible to covalent and noncovalent aggregation under moderate heat treatment (63 °C, 30 min). Blocked thiol group and reduced hydrophobicity due to hindering of hydrophobic residues by bound PCB, as well as the heat-induced transition of β-sheet to α-helix, contributed to the low susceptibility of BLG–PCB to aggregation. BLG–PCB has a higher resistance to pepsin and pancreatin digestion than BLG and unaltered IgE-binding properties. The improved functional properties of BLG–PCB make it a useful ingredient in the food industry.
PB  - Elsevier
T2  - Food Hydrocolloids
T1  - Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating
VL  - 123
SP  - 107169
DO  - 10.1016/j.foodhyd.2021.107169
ER  - 
@article{
author = "Radomirović, Mirjana Ž. and Minić, Simeon L. and Stanić-Vučinić, Dragana and Nikolić, Milan and Van Haute, Sam and Rajković, Andreja and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "β-lactoglobulin (BLG) is a major whey protein with numerous techno-functional properties desirable for the food industry. Phycocyanobilin (PCB), a bioactive pigment of Arthrospira platensis with health-promoting effects, covalently binds to BLG at physiological pH. This study investigated the effects of this covalent modification on BLG functional properties. The BLG–PCB adduct possesses enhanced antioxidant properties, and bound PCB protects BLG against free radical-induced oxidation. Despite the similar thermal stabilities of BLG and BLG–PCB, BLG–PCB is less susceptible to covalent and noncovalent aggregation under moderate heat treatment (63 °C, 30 min). Blocked thiol group and reduced hydrophobicity due to hindering of hydrophobic residues by bound PCB, as well as the heat-induced transition of β-sheet to α-helix, contributed to the low susceptibility of BLG–PCB to aggregation. BLG–PCB has a higher resistance to pepsin and pancreatin digestion than BLG and unaltered IgE-binding properties. The improved functional properties of BLG–PCB make it a useful ingredient in the food industry.",
publisher = "Elsevier",
journal = "Food Hydrocolloids",
title = "Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating",
volume = "123",
pages = "107169",
doi = "10.1016/j.foodhyd.2021.107169"
}
Radomirović, M. Ž., Minić, S. L., Stanić-Vučinić, D., Nikolić, M., Van Haute, S., Rajković, A.,& Ćirković-Veličković, T.. (2022). Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating. in Food Hydrocolloids
Elsevier., 123, 107169.
https://doi.org/10.1016/j.foodhyd.2021.107169
Radomirović MŽ, Minić SL, Stanić-Vučinić D, Nikolić M, Van Haute S, Rajković A, Ćirković-Veličković T. Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating. in Food Hydrocolloids. 2022;123:107169.
doi:10.1016/j.foodhyd.2021.107169 .
Radomirović, Mirjana Ž., Minić, Simeon L., Stanić-Vučinić, Dragana, Nikolić, Milan, Van Haute, Sam, Rajković, Andreja, Ćirković-Veličković, Tanja, "Phycocyanobilin-modified β-lactoglobulin exhibits increased antioxidant properties and stability to digestion and heating" in Food Hydrocolloids, 123 (2022):107169,
https://doi.org/10.1016/j.foodhyd.2021.107169 . .
2
7
7

Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes

Simović, Ana; Combet, Sophie; Ćirković-Veličković, Tanja; Nikolic, Milan; Minić, Simeon L.

(Elsevier, 2022)

TY  - JOUR
AU  - Simović, Ana
AU  - Combet, Sophie
AU  - Ćirković-Veličković, Tanja
AU  - Nikolic, Milan
AU  - Minić, Simeon L.
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5002
AB  - This study aimed to characterise the stability of R-phycoerythrin (R-PE), a vivid natural colourant with emerging
potential for application in the food industry. High-quality (A560/A280 ≥ 5), native (α-helix content 75%) R-PE
was purified from commercial dried Nori (Porphyra sp.) flakes. Thermal unfolding revealed two transitions (at 56
and 72 ◦C), ascribed to different protein subunits. Contrary to elevated temperature, high-pressure (HP) treatment showed significant advantages: The R-PE unfolding was partly reversible and the colour bleaching was
minimal. Binding of Cu2+ (6.3 × 105 M− 1
) and Zn2+ (1.7 × 103 M− 1
) influenced conformational changes in the
protein tetrapyrrole chromophore without affecting R-PE structure and stability (colour). The results give new
insights into the stability of R-PE suggesting its usefulness for the replacement of toxic synthetic dyes. Preservation of the red colour of R-PE could be considered in fortified food and beverages by HP processing. R-PE may
act as a biosensor for Cu2+ in aquatic systems.
PB  - Elsevier
T2  - Food Chemistry
T1  - Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes
VL  - 374
IS  - 131780
DO  - 10.1016/j.foodchem.2021.131780
ER  - 
@article{
author = "Simović, Ana and Combet, Sophie and Ćirković-Veličković, Tanja and Nikolic, Milan and Minić, Simeon L.",
year = "2022",
abstract = "This study aimed to characterise the stability of R-phycoerythrin (R-PE), a vivid natural colourant with emerging
potential for application in the food industry. High-quality (A560/A280 ≥ 5), native (α-helix content 75%) R-PE
was purified from commercial dried Nori (Porphyra sp.) flakes. Thermal unfolding revealed two transitions (at 56
and 72 ◦C), ascribed to different protein subunits. Contrary to elevated temperature, high-pressure (HP) treatment showed significant advantages: The R-PE unfolding was partly reversible and the colour bleaching was
minimal. Binding of Cu2+ (6.3 × 105 M− 1
) and Zn2+ (1.7 × 103 M− 1
) influenced conformational changes in the
protein tetrapyrrole chromophore without affecting R-PE structure and stability (colour). The results give new
insights into the stability of R-PE suggesting its usefulness for the replacement of toxic synthetic dyes. Preservation of the red colour of R-PE could be considered in fortified food and beverages by HP processing. R-PE may
act as a biosensor for Cu2+ in aquatic systems.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes",
volume = "374",
number = "131780",
doi = "10.1016/j.foodchem.2021.131780"
}
Simović, A., Combet, S., Ćirković-Veličković, T., Nikolic, M.,& Minić, S. L.. (2022). Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes. in Food Chemistry
Elsevier., 374(131780).
https://doi.org/10.1016/j.foodchem.2021.131780
Simović A, Combet S, Ćirković-Veličković T, Nikolic M, Minić SL. Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes. in Food Chemistry. 2022;374(131780).
doi:10.1016/j.foodchem.2021.131780 .
Simović, Ana, Combet, Sophie, Ćirković-Veličković, Tanja, Nikolic, Milan, Minić, Simeon L., "Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes" in Food Chemistry, 374, no. 131780 (2022),
https://doi.org/10.1016/j.foodchem.2021.131780 . .
1
3
2

Supplementary data for the article: Simović, A.; Combet, S.; Ćirković-Veličković, T.; Nikolic, M.; Minić, S. L. Probing the Stability of the Food Colourant R-Phycoerythrin from Dried Nori Flakes. Food Chemistry 2022, 374 (131780). https://doi.org/10.1016/j.foodchem.2021.131780.

Simović, Ana; Combet, Sophie; Ćirković-Veličković, Tanja; Nikolic, Milan; Minić, Simeon L.

(Elsevier, 2022)

TY  - DATA
AU  - Simović, Ana
AU  - Combet, Sophie
AU  - Ćirković-Veličković, Tanja
AU  - Nikolic, Milan
AU  - Minić, Simeon L.
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5003
PB  - Elsevier
T2  - Food Chemistry
T1  - Supplementary data for the article: Simović, A.; Combet, S.; Ćirković-Veličković, T.; Nikolic, M.; Minić, S. L. Probing the Stability of the Food Colourant R-Phycoerythrin from Dried Nori Flakes. Food Chemistry 2022, 374 (131780). https://doi.org/10.1016/j.foodchem.2021.131780.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5003
ER  - 
@misc{
author = "Simović, Ana and Combet, Sophie and Ćirković-Veličković, Tanja and Nikolic, Milan and Minić, Simeon L.",
year = "2022",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Supplementary data for the article: Simović, A.; Combet, S.; Ćirković-Veličković, T.; Nikolic, M.; Minić, S. L. Probing the Stability of the Food Colourant R-Phycoerythrin from Dried Nori Flakes. Food Chemistry 2022, 374 (131780). https://doi.org/10.1016/j.foodchem.2021.131780.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5003"
}
Simović, A., Combet, S., Ćirković-Veličković, T., Nikolic, M.,& Minić, S. L.. (2022). Supplementary data for the article: Simović, A.; Combet, S.; Ćirković-Veličković, T.; Nikolic, M.; Minić, S. L. Probing the Stability of the Food Colourant R-Phycoerythrin from Dried Nori Flakes. Food Chemistry 2022, 374 (131780). https://doi.org/10.1016/j.foodchem.2021.131780.. in Food Chemistry
Elsevier..
https://hdl.handle.net/21.15107/rcub_cherry_5003
Simović A, Combet S, Ćirković-Veličković T, Nikolic M, Minić SL. Supplementary data for the article: Simović, A.; Combet, S.; Ćirković-Veličković, T.; Nikolic, M.; Minić, S. L. Probing the Stability of the Food Colourant R-Phycoerythrin from Dried Nori Flakes. Food Chemistry 2022, 374 (131780). https://doi.org/10.1016/j.foodchem.2021.131780.. in Food Chemistry. 2022;.
https://hdl.handle.net/21.15107/rcub_cherry_5003 .
Simović, Ana, Combet, Sophie, Ćirković-Veličković, Tanja, Nikolic, Milan, Minić, Simeon L., "Supplementary data for the article: Simović, A.; Combet, S.; Ćirković-Veličković, T.; Nikolic, M.; Minić, S. L. Probing the Stability of the Food Colourant R-Phycoerythrin from Dried Nori Flakes. Food Chemistry 2022, 374 (131780). https://doi.org/10.1016/j.foodchem.2021.131780." in Food Chemistry (2022),
https://hdl.handle.net/21.15107/rcub_cherry_5003 .

Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain

Simović, Ana; Radomirović, Mirjana Ž.; Gligorijević, Nikola; Stanić-Vučinić, Dragana; Minić, Simeon L.; Nikolić, Milan; Ćirković-Veličković, Tanja

(Faculty of Chemistry, Serbian Biochemical Society, 2022)

TY  - CONF
AU  - Simović, Ana
AU  - Radomirović, Mirjana Ž.
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Minić, Simeon L.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5520
AB  - The emergence of the coronavirus SARS-CoV-2 has attracted attention of the whole scientific community. The SARS-CoV-2 spike (S) protein plays the most important role in viral attachment to host receptor angiotensin-converting enzyme 2 (ACE2), via the receptor-binding domain (RBD), fusion and entry into the host, and it serves as a target for the development of antibodies, entry inhibitors and vaccines. It has been demonstrated that phycocyanobilin (PCB), a bioactive open-chain tetrapyrrole chromophore of phycocyanin (PC), chromoprotein derived from the cyanobacterium Arthrospira platensis, can bind a plethora of different proteins, both in a noncovalent and covalent manner. This study aimed to investigate interactions of PCB with S protein and RBD respectively. Electrophoretic techniques, fluorescence spectroscopy, and inhibition of S–PCB and RBD–PCB covalent adduct formation using iodoacetamide and N-ethylmaleimide, were employed to examine interactions of PCB with S protein and RBD, while the effects of PCB binding on RBD structure were studied by CD spectroscopy. SDS-PAGE with Zn2+ staining has revealed that PCB covalently binds to both S protein and RBD, via free cysteine residues. Binding constants determined by the fluorescence quenching method were: 2.1×107 M–1 for PCB and S protein and 8.4×104 M–1 for PCB and RBD. Far-UV circular dichroism spectra showed that the binding of PCB influences RBD structure by decreasing the disordered structure content. Due to moderately strong noncovalent interactions of PCB with S protein and RBD, as well as covalent adducts formation, it may exert one of its many bioactive effects via impact on S protein binding to ACE2 receptor.
PB  - Faculty of Chemistry, Serbian Biochemical Society
C3  - Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia
T1  - Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain
SP  - 130
EP  - 131
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5520
ER  - 
@conference{
author = "Simović, Ana and Radomirović, Mirjana Ž. and Gligorijević, Nikola and Stanić-Vučinić, Dragana and Minić, Simeon L. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "The emergence of the coronavirus SARS-CoV-2 has attracted attention of the whole scientific community. The SARS-CoV-2 spike (S) protein plays the most important role in viral attachment to host receptor angiotensin-converting enzyme 2 (ACE2), via the receptor-binding domain (RBD), fusion and entry into the host, and it serves as a target for the development of antibodies, entry inhibitors and vaccines. It has been demonstrated that phycocyanobilin (PCB), a bioactive open-chain tetrapyrrole chromophore of phycocyanin (PC), chromoprotein derived from the cyanobacterium Arthrospira platensis, can bind a plethora of different proteins, both in a noncovalent and covalent manner. This study aimed to investigate interactions of PCB with S protein and RBD respectively. Electrophoretic techniques, fluorescence spectroscopy, and inhibition of S–PCB and RBD–PCB covalent adduct formation using iodoacetamide and N-ethylmaleimide, were employed to examine interactions of PCB with S protein and RBD, while the effects of PCB binding on RBD structure were studied by CD spectroscopy. SDS-PAGE with Zn2+ staining has revealed that PCB covalently binds to both S protein and RBD, via free cysteine residues. Binding constants determined by the fluorescence quenching method were: 2.1×107 M–1 for PCB and S protein and 8.4×104 M–1 for PCB and RBD. Far-UV circular dichroism spectra showed that the binding of PCB influences RBD structure by decreasing the disordered structure content. Due to moderately strong noncovalent interactions of PCB with S protein and RBD, as well as covalent adducts formation, it may exert one of its many bioactive effects via impact on S protein binding to ACE2 receptor.",
publisher = "Faculty of Chemistry, Serbian Biochemical Society",
journal = "Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia",
title = "Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain",
pages = "130-131",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5520"
}
Simović, A., Radomirović, M. Ž., Gligorijević, N., Stanić-Vučinić, D., Minić, S. L., Nikolić, M.,& Ćirković-Veličković, T.. (2022). Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain. in Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia
Faculty of Chemistry, Serbian Biochemical Society., 130-131.
https://hdl.handle.net/21.15107/rcub_cherry_5520
Simović A, Radomirović MŽ, Gligorijević N, Stanić-Vučinić D, Minić SL, Nikolić M, Ćirković-Veličković T. Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain. in Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia. 2022;:130-131.
https://hdl.handle.net/21.15107/rcub_cherry_5520 .
Simović, Ana, Radomirović, Mirjana Ž., Gligorijević, Nikola, Stanić-Vučinić, Dragana, Minić, Simeon L., Nikolić, Milan, Ćirković-Veličković, Tanja, "Noncovalent and covalent binding of phycocyanobilin to S protein of SARS-CoV-2 and its receptor-binding domain" in Serbian Biochemical Society Eleventh Conference, Scientific meeting of an international character, September 22nd and 23rd, 2022, Novi Sad, Serbia (2022):130-131,
https://hdl.handle.net/21.15107/rcub_cherry_5520 .

Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting

Đukić, Teodora; Smiljanić, Katarina; Mihailović, Jelena; Prodić, Ivana; Apostolović, Danijela; Liu, Shu-Hua; Epstein, Michelle M.; van Hage, Marianne; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(MDPI, 2022)

TY  - JOUR
AU  - Đukić, Teodora
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Liu, Shu-Hua
AU  - Epstein, Michelle M.
AU  - van Hage, Marianne
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5781
AB  - : Post-translational modifications (PTMs) are covalent changes occurring on amino acid side
chains of proteins and yet are neglected structural and functional aspects of protein architecture. The
objective was to detect differences in PTM profiles that take place after roasting using open PTM
search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on
readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications
was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing
protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative
profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms
of modification versatility and extent. The most frequent PTM was methionine oxidation, especially
in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation
(Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ
in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study
provides a better understanding of how roasting impacts the PTM profile of major peanut allergens
and provides a good foundation for further exploration of PTMs
PB  - MDPI
T2  - Foods
T1  - Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting
VL  - 11
IS  - 24
SP  - 3993
DO  - 10.3390/foods11243993
ER  - 
@article{
author = "Đukić, Teodora and Smiljanić, Katarina and Mihailović, Jelena and Prodić, Ivana and Apostolović, Danijela and Liu, Shu-Hua and Epstein, Michelle M. and van Hage, Marianne and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2022",
abstract = ": Post-translational modifications (PTMs) are covalent changes occurring on amino acid side
chains of proteins and yet are neglected structural and functional aspects of protein architecture. The
objective was to detect differences in PTM profiles that take place after roasting using open PTM
search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on
readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications
was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing
protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative
profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms
of modification versatility and extent. The most frequent PTM was methionine oxidation, especially
in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation
(Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ
in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study
provides a better understanding of how roasting impacts the PTM profile of major peanut allergens
and provides a good foundation for further exploration of PTMs",
publisher = "MDPI",
journal = "Foods",
title = "Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting",
volume = "11",
number = "24",
pages = "3993",
doi = "10.3390/foods11243993"
}
Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S., Epstein, M. M., van Hage, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. in Foods
MDPI., 11(24), 3993.
https://doi.org/10.3390/foods11243993
Đukić T, Smiljanić K, Mihailović J, Prodić I, Apostolović D, Liu S, Epstein MM, van Hage M, Stanić-Vučinić D, Ćirković-Veličković T. Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. in Foods. 2022;11(24):3993.
doi:10.3390/foods11243993 .
Đukić, Teodora, Smiljanić, Katarina, Mihailović, Jelena, Prodić, Ivana, Apostolović, Danijela, Liu, Shu-Hua, Epstein, Michelle M., van Hage, Marianne, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting" in Foods, 11, no. 24 (2022):3993,
https://doi.org/10.3390/foods11243993 . .

Производња рекомбинантних антигена и развој одрживих тестова за Covid-19

Ćirković-Veličković, Tanja

(Београд : Српска академија наука и уметности, 2022)

TY  - CONF
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5778
AB  - Нови корона вирус (SARS CoV-2) је нови инфективни агенс за хуману популацију и веома је брзо детектован у великом броју земаља. Брзо ширење, одсуство имунитета на овај вирус и одсуство поузданих тестова за детекцију вируса у тренутку избијања пандемије су болест изазвану овим вирусом брзо претворили у здравствени и друштвени проблем највишег приоритета на глобалном нивоу. Иако су највеће биотехнолошке компаније убрзано почеле са развојем и масовном производњом дијагностичких тестова и вакцина, њихова доступност у тренуцима највеће потражње је и даље недовољна, а цене истих су лимитирајући фактор за бољу контролу болести и ширења пандемије. Тестови имају и своја ограничења, посебно када су у питању антигенски тестови, тако да се и даље ради на унапређењу осетљивости истих. У фокусу наших истраживања је развој дијагностичких и серолошких тестова за COVID-19. Дијагностички тестови детектују делове вируса: генетског материјала вируса , односно протеинске компоненте вируса. Серолошки тестови који детектују присуство антитела на протеине вируса. Важна компенента ових тестова је рекомбинанто произведен протеин. Истраживачки тим Хемијског факултета је до сада произвео рекомбинантне протеине шиљка и нуклеокапсида за потребе развоја серолошког теста и N протеин високе чистоће на великој скали за потребе добијања специфичких антитела и развоја антигенског теста. Добијена високо специфична поликлонска антитела на N протеин вируса из имунизованих животиња, биће употребљена за дизајн основног сендвич ЕЛИСА теста за детекцију SARS CoV-2 вируса на бази препознавања N-протеина вируса.  Oчекује се даље унапређење осетљивости теста применом различитих техника, као што су имобилисана специфична антитела на принципу имуноафинитетног ЕЛИСА теста што ће омогућити хватање вирусних антигена у хуманим телесним течностима попут крви, урина и пљувачке, и њихово даље концентрисање, што са једне стране повећава могућност за тачан резултат а са друге стране шири репертоар врсте узорака.
PB  - Београд : Српска академија наука и уметности
C3  - COVID-19 пандемије: поруке, нова сазнања и дилеме
T1  - Производња рекомбинантних антигена и развој одрживих тестова за Covid-19
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5778
ER  - 
@conference{
author = "Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Нови корона вирус (SARS CoV-2) је нови инфективни агенс за хуману популацију и веома је брзо детектован у великом броју земаља. Брзо ширење, одсуство имунитета на овај вирус и одсуство поузданих тестова за детекцију вируса у тренутку избијања пандемије су болест изазвану овим вирусом брзо претворили у здравствени и друштвени проблем највишег приоритета на глобалном нивоу. Иако су највеће биотехнолошке компаније убрзано почеле са развојем и масовном производњом дијагностичких тестова и вакцина, њихова доступност у тренуцима највеће потражње је и даље недовољна, а цене истих су лимитирајући фактор за бољу контролу болести и ширења пандемије. Тестови имају и своја ограничења, посебно када су у питању антигенски тестови, тако да се и даље ради на унапређењу осетљивости истих. У фокусу наших истраживања је развој дијагностичких и серолошких тестова за COVID-19. Дијагностички тестови детектују делове вируса: генетског материјала вируса , односно протеинске компоненте вируса. Серолошки тестови који детектују присуство антитела на протеине вируса. Важна компенента ових тестова је рекомбинанто произведен протеин. Истраживачки тим Хемијског факултета је до сада произвео рекомбинантне протеине шиљка и нуклеокапсида за потребе развоја серолошког теста и N протеин високе чистоће на великој скали за потребе добијања специфичких антитела и развоја антигенског теста. Добијена високо специфична поликлонска антитела на N протеин вируса из имунизованих животиња, биће употребљена за дизајн основног сендвич ЕЛИСА теста за детекцију SARS CoV-2 вируса на бази препознавања N-протеина вируса.  Oчекује се даље унапређење осетљивости теста применом различитих техника, као што су имобилисана специфична антитела на принципу имуноафинитетног ЕЛИСА теста што ће омогућити хватање вирусних антигена у хуманим телесним течностима попут крви, урина и пљувачке, и њихово даље концентрисање, што са једне стране повећава могућност за тачан резултат а са друге стране шири репертоар врсте узорака.",
publisher = "Београд : Српска академија наука и уметности",
journal = "COVID-19 пандемије: поруке, нова сазнања и дилеме",
title = "Производња рекомбинантних антигена и развој одрживих тестова за Covid-19",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5778"
}
Ćirković-Veličković, T.. (2022). Производња рекомбинантних антигена и развој одрживих тестова за Covid-19. in COVID-19 пандемије: поруке, нова сазнања и дилеме
Београд : Српска академија наука и уметности..
https://hdl.handle.net/21.15107/rcub_cherry_5778
Ćirković-Veličković T. Производња рекомбинантних антигена и развој одрживих тестова за Covid-19. in COVID-19 пандемије: поруке, нова сазнања и дилеме. 2022;.
https://hdl.handle.net/21.15107/rcub_cherry_5778 .
Ćirković-Veličković, Tanja, "Производња рекомбинантних антигена и развој одрживих тестова за Covid-19" in COVID-19 пандемије: поруке, нова сазнања и дилеме (2022),
https://hdl.handle.net/21.15107/rcub_cherry_5778 .

SARS CoV-2 nucleocapsid-based diagnostic tests and serological response in allergic children

Ćirković-Veličković, Tanja; Radomirović, Mirjana; Simović, Ana; Jovanović, Vesna B.; Ćujić, Danica R.; Gnjatović, Marija Lj.; Stojanović, Marijana

(2022)

TY  - CONF
AU  - Ćirković-Veličković, Tanja
AU  - Radomirović, Mirjana
AU  - Simović, Ana
AU  - Jovanović, Vesna B.
AU  - Ćujić, Danica R.
AU  - Gnjatović, Marija Lj.
AU  - Stojanović, Marijana
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5777
AB  - RT-PCR remains the primary method of diagnosing SARS-CoV-2. Serological diagnosis of COVID-19 is simple and does not require complex techniques and equipment, rendering it suitable for rapid detection and massive screening. However, serological tests cannot confirm SARS-CoV-2, and results will be false negative when antibody concentrations fall below detection limit. Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARS CoV-2) infection. Antigen-based tests show high specificity, but sensitivity is relatively low. For development and further improvement of both serological and antigen-based tests, availability of recombinantly producted SARS CoV-2 antigens is needed and during the periods of high demend in the pandemic, it was a limited factor both for research and diagnostic tests production by national producers of tests. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production. SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58-419 aa) was expressed in E. coli in soluble form, purified and characterized biochemically and immunologically. Purified rfNP has secondary structure of full-length recombinant N protein, with high percentage of disordered structure (34.2%) and of beta-sheet (40.7%). rfNP was tested in immunoblot using sera of COVID-19 convalescent patients. Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection. ELISA was optimized with sera of RT-PCR confirmed positive symptomatic patients and healthy individuals. IgG detection sensitivity was 96% (47/50) and specificity 97% (67/68), while IgM detection was slightly lower (94% and 96.5%, respectively). Application of serological ELISA for seropositivity detection in 200 allergic children in comparison to non-allergic did not show a bias towards any of the tested groups.  Furthermore, we have optimized production of rfNP at a large scale to raise specific antibodies to N-protein in rabbit and mice and develop an in house ELISA for quantification of N protein in biological fluids. Test was clinically validated in 200 PCR positive patients and showed a sensitivity of around 50%.
C3  - International Congress on Molecular Immunology and Allergology (IMAC-2022), Moscow, December 1-3, 2022
T1  - SARS CoV-2 nucleocapsid-based diagnostic tests and serological response in allergic children
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5777
ER  - 
@conference{
author = "Ćirković-Veličković, Tanja and Radomirović, Mirjana and Simović, Ana and Jovanović, Vesna B. and Ćujić, Danica R. and Gnjatović, Marija Lj. and Stojanović, Marijana",
year = "2022",
abstract = "RT-PCR remains the primary method of diagnosing SARS-CoV-2. Serological diagnosis of COVID-19 is simple and does not require complex techniques and equipment, rendering it suitable for rapid detection and massive screening. However, serological tests cannot confirm SARS-CoV-2, and results will be false negative when antibody concentrations fall below detection limit. Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARS CoV-2) infection. Antigen-based tests show high specificity, but sensitivity is relatively low. For development and further improvement of both serological and antigen-based tests, availability of recombinantly producted SARS CoV-2 antigens is needed and during the periods of high demend in the pandemic, it was a limited factor both for research and diagnostic tests production by national producers of tests. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production. SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58-419 aa) was expressed in E. coli in soluble form, purified and characterized biochemically and immunologically. Purified rfNP has secondary structure of full-length recombinant N protein, with high percentage of disordered structure (34.2%) and of beta-sheet (40.7%). rfNP was tested in immunoblot using sera of COVID-19 convalescent patients. Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection. ELISA was optimized with sera of RT-PCR confirmed positive symptomatic patients and healthy individuals. IgG detection sensitivity was 96% (47/50) and specificity 97% (67/68), while IgM detection was slightly lower (94% and 96.5%, respectively). Application of serological ELISA for seropositivity detection in 200 allergic children in comparison to non-allergic did not show a bias towards any of the tested groups.  Furthermore, we have optimized production of rfNP at a large scale to raise specific antibodies to N-protein in rabbit and mice and develop an in house ELISA for quantification of N protein in biological fluids. Test was clinically validated in 200 PCR positive patients and showed a sensitivity of around 50%.",
journal = "International Congress on Molecular Immunology and Allergology (IMAC-2022), Moscow, December 1-3, 2022",
title = "SARS CoV-2 nucleocapsid-based diagnostic tests and serological response in allergic children",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5777"
}
Ćirković-Veličković, T., Radomirović, M., Simović, A., Jovanović, V. B., Ćujić, D. R., Gnjatović, M. Lj.,& Stojanović, M.. (2022). SARS CoV-2 nucleocapsid-based diagnostic tests and serological response in allergic children. in International Congress on Molecular Immunology and Allergology (IMAC-2022), Moscow, December 1-3, 2022.
https://hdl.handle.net/21.15107/rcub_cherry_5777
Ćirković-Veličković T, Radomirović M, Simović A, Jovanović VB, Ćujić DR, Gnjatović ML, Stojanović M. SARS CoV-2 nucleocapsid-based diagnostic tests and serological response in allergic children. in International Congress on Molecular Immunology and Allergology (IMAC-2022), Moscow, December 1-3, 2022. 2022;.
https://hdl.handle.net/21.15107/rcub_cherry_5777 .
Ćirković-Veličković, Tanja, Radomirović, Mirjana, Simović, Ana, Jovanović, Vesna B., Ćujić, Danica R., Gnjatović, Marija Lj., Stojanović, Marijana, "SARS CoV-2 nucleocapsid-based diagnostic tests and serological response in allergic children" in International Congress on Molecular Immunology and Allergology (IMAC-2022), Moscow, December 1-3, 2022 (2022),
https://hdl.handle.net/21.15107/rcub_cherry_5777 .

Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein

Radomirović, Mirjana Ž.; Simović, Ana; Udovički, Božidar D.; Krstić-Ristivojević, Maja V.; Sabljić, Ljiljana Z.; Lukić, Ivana D.; Glamočlija, Sofija Đ.; Ćujić, Danica R.; Gnjatović, Marija Lj.; Stojanović, Marijana M.; Stanić-Vučinić, Dragana; Radosavljević, Jelena; Ćirković-Veličković, Tanja

(Beograd : Srpsko hemijsko društvo, 2022)

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Simović, Ana
AU  - Udovički, Božidar D.
AU  - Krstić-Ristivojević, Maja V.
AU  - Sabljić, Ljiljana Z.
AU  - Lukić, Ivana D.
AU  - Glamočlija, Sofija Đ.
AU  - Ćujić, Danica R.
AU  - Gnjatović, Marija Lj.
AU  - Stojanović, Marijana M.
AU  - Stanić-Vučinić, Dragana
AU  - Radosavljević, Jelena
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5361
AB  - Ta na dijagnoza ljudi sa sumnjom na infekciju SARS-CoV-2 je od suštinskog zna aja za
suzbijanje globalnog širenja COVID-19. Prisustvo SARS-CoV-2 može se otkriti RT-PCRom (otkriva RNK virusa) ili detekcijom prisustva virusnih antigena u biološkim te nostima
ELISA-om ili sli nom tehnikom koje koriste antitela razvijena u životinjama. Cilj studije
je bio uspostavljanje kvantitativnog testa koji se zasniva na koriš enju poliklonskih seruma
za rutinsko odre ivanje koncentracije SARS-CoV-2 nukleokapsidnog proteina merenjam
apsorbancije u standardnoj mikrotitarskoj plo ici sa 96 bunara. Za potrebe razvoja testa
proizveden je rekombinantni N-protein i koriš en za proizvodnju antiseruma u miševima i
ze evima. Proizvedeni antiserumi su pre iš eni i odre en im je titar. Poliklonskiantiserumi
visokog afiniteta specifi ni za N-protein koriš eni su za razvoj ELISA testa specifi nog za
ovaj protein. Test se zasniva na koriš enju poliklonskih seruma miševa koji su adherirani
na dno bunara mikrotitarske plo ice za hvatanje N-proteina iz uzorka. Razli ite
koncentracije rekombinantnog N-proteina su koriš ene za standardnu krivu za
kvantifikaciju proteina. N-protein vezan za antitela miševa je detektovan ze jim
poliklonskim serumom i anti-ze jim antitelom povezanim sa enzimom koji obezbe uje
spektrofotometrijsko merenje. Uspešno smo razvili prototip ELISA testa za kvantifikaciju
N-proteina sa granicom detekcije u opsegu od ng/mL. Prose na vrednost LOD za prototip
ELISA testa za detekciju N-proteina je 9,2 ng/mL, dok je prose na vrednost LOQ
10,2 ng/mL. Pokazali smo da su proizvedeni poliklonski antiserumi pogodni za detekciju
N-proteina sa sli nim ili boljim afinitetom i specifi noš u od komercijalnih antitela.
Štaviše, prototip ELISA testa se može koristiti sa zadovoljavaju om pouzdanoš u za
kvantifikaciju N-proteina u uzorcima bogatim proteinima, poput ljudskih seruma.
AB  - The accurate diagnosis of people with suspected infection with the SARS-CoV-2 is
essential to curb the global spread of COVID-19. The presence of SARS-CoV-2 can be
detected by RT-PCR (it detects RNA of the virus) or by the presence of viral antigens in
biological fluids in ELISA or similar techniques using antibodies developed in animals.
The aim of the study was the establishment of a quantitative polyclonal sera-based test for
routine measurement of the concentration of SARS CoV-2 nucleocapsid protein using
absorbance measurement in a standard 96-well microtiter plate. For the purposes of the test
development, recombinant N protein was produced and used for the production of mice
and rabbit antisera. Produced antisera were purified and titer was determined. High-affinity
polyclonal N-protein specific antisera were used for N-protein specific ELISA test
development. The test is based on mice polyclonal sera adhered to microtiter plate bottom
for the capture of the N protein from the specimen. Various concentrations of the
recombinant N-protein were used to generate a standard curve for protein quantification.
The N-protein bound to the mice antibodies was detected with rabbit polyclonal sera and
anti-rabbit antibody coupled to an enzyme that provides spectrophotometric measurement.
We have successfully developed the prototype ELISA for the quantification of N-protein
with the detection limit being in the range of ng/mL. The average LOD value for the
prototype ELISA was determined to be 9.2 ng/mL, while the average LOQ value was
10.2 ng/mL. We have demonstrated that produced polyclonal antisera are suitable for the
detection of N-protein with affinity and specificity similar to, or better than commercial
antibodies. Furthermore, the prototype ELISA can be used with satisfactory confidence for
quantification of the N-protein in protein-rich samples, similar to human sera.
PB  - Beograd : Srpsko hemijsko društvo
C3  - 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine
T1  - Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein
T1  - Development of SARS-CoV-2 N-protein specific capture ELISA
SP  - 65
EP  - 66
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5361
ER  - 
@conference{
author = "Radomirović, Mirjana Ž. and Simović, Ana and Udovički, Božidar D. and Krstić-Ristivojević, Maja V. and Sabljić, Ljiljana Z. and Lukić, Ivana D. and Glamočlija, Sofija Đ. and Ćujić, Danica R. and Gnjatović, Marija Lj. and Stojanović, Marijana M. and Stanić-Vučinić, Dragana and Radosavljević, Jelena and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Ta na dijagnoza ljudi sa sumnjom na infekciju SARS-CoV-2 je od suštinskog zna aja za
suzbijanje globalnog širenja COVID-19. Prisustvo SARS-CoV-2 može se otkriti RT-PCRom (otkriva RNK virusa) ili detekcijom prisustva virusnih antigena u biološkim te nostima
ELISA-om ili sli nom tehnikom koje koriste antitela razvijena u životinjama. Cilj studije
je bio uspostavljanje kvantitativnog testa koji se zasniva na koriš enju poliklonskih seruma
za rutinsko odre ivanje koncentracije SARS-CoV-2 nukleokapsidnog proteina merenjam
apsorbancije u standardnoj mikrotitarskoj plo ici sa 96 bunara. Za potrebe razvoja testa
proizveden je rekombinantni N-protein i koriš en za proizvodnju antiseruma u miševima i
ze evima. Proizvedeni antiserumi su pre iš eni i odre en im je titar. Poliklonskiantiserumi
visokog afiniteta specifi ni za N-protein koriš eni su za razvoj ELISA testa specifi nog za
ovaj protein. Test se zasniva na koriš enju poliklonskih seruma miševa koji su adherirani
na dno bunara mikrotitarske plo ice za hvatanje N-proteina iz uzorka. Razli ite
koncentracije rekombinantnog N-proteina su koriš ene za standardnu krivu za
kvantifikaciju proteina. N-protein vezan za antitela miševa je detektovan ze jim
poliklonskim serumom i anti-ze jim antitelom povezanim sa enzimom koji obezbe uje
spektrofotometrijsko merenje. Uspešno smo razvili prototip ELISA testa za kvantifikaciju
N-proteina sa granicom detekcije u opsegu od ng/mL. Prose na vrednost LOD za prototip
ELISA testa za detekciju N-proteina je 9,2 ng/mL, dok je prose na vrednost LOQ
10,2 ng/mL. Pokazali smo da su proizvedeni poliklonski antiserumi pogodni za detekciju
N-proteina sa sli nim ili boljim afinitetom i specifi noš u od komercijalnih antitela.
Štaviše, prototip ELISA testa se može koristiti sa zadovoljavaju om pouzdanoš u za
kvantifikaciju N-proteina u uzorcima bogatim proteinima, poput ljudskih seruma., The accurate diagnosis of people with suspected infection with the SARS-CoV-2 is
essential to curb the global spread of COVID-19. The presence of SARS-CoV-2 can be
detected by RT-PCR (it detects RNA of the virus) or by the presence of viral antigens in
biological fluids in ELISA or similar techniques using antibodies developed in animals.
The aim of the study was the establishment of a quantitative polyclonal sera-based test for
routine measurement of the concentration of SARS CoV-2 nucleocapsid protein using
absorbance measurement in a standard 96-well microtiter plate. For the purposes of the test
development, recombinant N protein was produced and used for the production of mice
and rabbit antisera. Produced antisera were purified and titer was determined. High-affinity
polyclonal N-protein specific antisera were used for N-protein specific ELISA test
development. The test is based on mice polyclonal sera adhered to microtiter plate bottom
for the capture of the N protein from the specimen. Various concentrations of the
recombinant N-protein were used to generate a standard curve for protein quantification.
The N-protein bound to the mice antibodies was detected with rabbit polyclonal sera and
anti-rabbit antibody coupled to an enzyme that provides spectrophotometric measurement.
We have successfully developed the prototype ELISA for the quantification of N-protein
with the detection limit being in the range of ng/mL. The average LOD value for the
prototype ELISA was determined to be 9.2 ng/mL, while the average LOQ value was
10.2 ng/mL. We have demonstrated that produced polyclonal antisera are suitable for the
detection of N-protein with affinity and specificity similar to, or better than commercial
antibodies. Furthermore, the prototype ELISA can be used with satisfactory confidence for
quantification of the N-protein in protein-rich samples, similar to human sera.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine",
title = "Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein, Development of SARS-CoV-2 N-protein specific capture ELISA",
pages = "65-66",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5361"
}
Radomirović, M. Ž., Simović, A., Udovički, B. D., Krstić-Ristivojević, M. V., Sabljić, L. Z., Lukić, I. D., Glamočlija, S. Đ., Ćujić, D. R., Gnjatović, M. Lj., Stojanović, M. M., Stanić-Vučinić, D., Radosavljević, J.,& Ćirković-Veličković, T.. (2022). Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein. in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine
Beograd : Srpsko hemijsko društvo., 65-66.
https://hdl.handle.net/21.15107/rcub_cherry_5361
Radomirović MŽ, Simović A, Udovički BD, Krstić-Ristivojević MV, Sabljić LZ, Lukić ID, Glamočlija SĐ, Ćujić DR, Gnjatović ML, Stojanović MM, Stanić-Vučinić D, Radosavljević J, Ćirković-Veličković T. Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein. in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine. 2022;:65-66.
https://hdl.handle.net/21.15107/rcub_cherry_5361 .
Radomirović, Mirjana Ž., Simović, Ana, Udovički, Božidar D., Krstić-Ristivojević, Maja V., Sabljić, Ljiljana Z., Lukić, Ivana D., Glamočlija, Sofija Đ., Ćujić, Danica R., Gnjatović, Marija Lj., Stojanović, Marijana M., Stanić-Vučinić, Dragana, Radosavljević, Jelena, Ćirković-Veličković, Tanja, "Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein" in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine (2022):65-66,
https://hdl.handle.net/21.15107/rcub_cherry_5361 .

Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein

Radomirović, Mirjana Ž.; Simović, Ana; Udovički, Božidar D.; Krstić-Ristivojević, Maja V.; Sabljić, Ljiljana Z.; Lukić, Ivana D.; Glamočlija, Sofija Đ.; Ćujić, Danica R.; Gnjatović, Marija Lj.; Stojanović, Marijana M.; Stanić-Vučinić, Dragana; Radosavljević, Jelena; Ćirković-Veličković, Tanja

(Beograd : Srpsko hemijsko društvo, 2022)

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Simović, Ana
AU  - Udovički, Božidar D.
AU  - Krstić-Ristivojević, Maja V.
AU  - Sabljić, Ljiljana Z.
AU  - Lukić, Ivana D.
AU  - Glamočlija, Sofija Đ.
AU  - Ćujić, Danica R.
AU  - Gnjatović, Marija Lj.
AU  - Stojanović, Marijana M.
AU  - Stanić-Vučinić, Dragana
AU  - Radosavljević, Jelena
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5362
AB  - Ta na dijagnoza ljudi sa sumnjom na infekciju SARS-CoV-2 je od suštinskog zna aja zasuzbijanje globalnog širenja COVID-19. Prisustvo SARS-CoV-2 može se otkriti RT-PCRom (otkriva RNK virusa) ili detekcijom prisustva virusnih antigena u biološkim te nostimaELISA-om ili sli nom tehnikom koje koriste antitela razvijena u životinjama. Cilj studijeje bio uspostavljanje kvantitativnog testa koji se zasniva na koriš enju poliklonskih serumaza rutinsko odre ivanje koncentracije SARS-CoV-2 nukleokapsidnog proteina merenjamapsorbancije u standardnoj mikrotitarskoj plo ici sa 96 bunara. Za potrebe razvoja testaproizveden je rekombinantni N-protein i koriš en za proizvodnju antiseruma u miševima ize evima. Proizvedeni antiserumi su pre iš eni i odre en im je titar. Poliklonskiantiserumivisokog afiniteta specifi ni za N-protein koriš eni su za razvoj ELISA testa specifi nog zaovaj protein. Test se zasniva na koriš enju poliklonskih seruma miševa koji su adheriranina dno bunara mikrotitarske plo ice za hvatanje N-proteina iz uzorka. Razli itekoncentracije rekombinantnog N-proteina su koriš ene za standardnu krivu zakvantifikaciju proteina. N-protein vezan za antitela miševa je detektovan ze jimpoliklonskim serumom i anti-ze jim antitelom povezanim sa enzimom koji obezbe ujespektrofotometrijsko merenje. Uspešno smo razvili prototip ELISA testa za kvantifikacijuN-proteina sa granicom detekcije u opsegu od ng/mL. Prose na vrednost LOD za prototipELISA testa za detekciju N-proteina je 9,2 ng/mL, dok je prose na vrednost LOQ10,2 ng/mL. Pokazali smo da su proizvedeni poliklonski antiserumi pogodni za detekcijuN-proteina sa sli nim ili boljim afinitetom i specifi noš u od komercijalnih antitela.Štaviše, prototip ELISA testa se može koristiti sa zadovoljavaju om pouzdanoš u zakvantifikaciju N-proteina u uzorcima bogatim proteinima, poput ljudskih seruma.
AB  - The accurate diagnosis of people with suspected infection with the SARS-CoV-2 isessential to curb the global spread of COVID-19. The presence of SARS-CoV-2 can bedetected by RT-PCR (it detects RNA of the virus) or by the presence of viral antigens inbiological fluids in ELISA or similar techniques using antibodies developed in animals.The aim of the study was the establishment of a quantitative polyclonal sera-based test forroutine measurement of the concentration of SARS CoV-2 nucleocapsid protein usingabsorbance measurement in a standard 96-well microtiter plate. For the purposes of the testdevelopment, recombinant N protein was produced and used for the production of miceand rabbit antisera. Produced antisera were purified and titer was determined. High-affinitypolyclonal N-protein specific antisera were used for N-protein specific ELISA testdevelopment. The test is based on mice polyclonal sera adhered to microtiter plate bottomfor the capture of the N protein from the specimen. Various concentrations of therecombinant N-protein were used to generate a standard curve for protein quantification.The N-protein bound to the mice antibodies was detected with rabbit polyclonal sera andanti-rabbit antibody coupled to an enzyme that provides spectrophotometric measurement.We have successfully developed the prototype ELISA for the quantification of N-proteinwith the detection limit being in the range of ng/mL. The average LOD value for theprototype ELISA was determined to be 9.2 ng/mL, while the average LOQ value was10.2 ng/mL. We have demonstrated that produced polyclonal antisera are suitable for thedetection of N-protein with affinity and specificity similar to, or better than commercialantibodies. Furthermore, the prototype ELISA can be used with satisfactory confidence forquantification of the N-protein in protein-rich samples, similar to human sera.
PB  - Beograd : Srpsko hemijsko društvo
C3  - 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine
T1  - Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein
T1  - Development of SARS-CoV-2 N-protein specific capture ELISA
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5362
ER  - 
@conference{
author = "Radomirović, Mirjana Ž. and Simović, Ana and Udovički, Božidar D. and Krstić-Ristivojević, Maja V. and Sabljić, Ljiljana Z. and Lukić, Ivana D. and Glamočlija, Sofija Đ. and Ćujić, Danica R. and Gnjatović, Marija Lj. and Stojanović, Marijana M. and Stanić-Vučinić, Dragana and Radosavljević, Jelena and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Ta na dijagnoza ljudi sa sumnjom na infekciju SARS-CoV-2 je od suštinskog zna aja zasuzbijanje globalnog širenja COVID-19. Prisustvo SARS-CoV-2 može se otkriti RT-PCRom (otkriva RNK virusa) ili detekcijom prisustva virusnih antigena u biološkim te nostimaELISA-om ili sli nom tehnikom koje koriste antitela razvijena u životinjama. Cilj studijeje bio uspostavljanje kvantitativnog testa koji se zasniva na koriš enju poliklonskih serumaza rutinsko odre ivanje koncentracije SARS-CoV-2 nukleokapsidnog proteina merenjamapsorbancije u standardnoj mikrotitarskoj plo ici sa 96 bunara. Za potrebe razvoja testaproizveden je rekombinantni N-protein i koriš en za proizvodnju antiseruma u miševima ize evima. Proizvedeni antiserumi su pre iš eni i odre en im je titar. Poliklonskiantiserumivisokog afiniteta specifi ni za N-protein koriš eni su za razvoj ELISA testa specifi nog zaovaj protein. Test se zasniva na koriš enju poliklonskih seruma miševa koji su adheriranina dno bunara mikrotitarske plo ice za hvatanje N-proteina iz uzorka. Razli itekoncentracije rekombinantnog N-proteina su koriš ene za standardnu krivu zakvantifikaciju proteina. N-protein vezan za antitela miševa je detektovan ze jimpoliklonskim serumom i anti-ze jim antitelom povezanim sa enzimom koji obezbe ujespektrofotometrijsko merenje. Uspešno smo razvili prototip ELISA testa za kvantifikacijuN-proteina sa granicom detekcije u opsegu od ng/mL. Prose na vrednost LOD za prototipELISA testa za detekciju N-proteina je 9,2 ng/mL, dok je prose na vrednost LOQ10,2 ng/mL. Pokazali smo da su proizvedeni poliklonski antiserumi pogodni za detekcijuN-proteina sa sli nim ili boljim afinitetom i specifi noš u od komercijalnih antitela.Štaviše, prototip ELISA testa se može koristiti sa zadovoljavaju om pouzdanoš u zakvantifikaciju N-proteina u uzorcima bogatim proteinima, poput ljudskih seruma., The accurate diagnosis of people with suspected infection with the SARS-CoV-2 isessential to curb the global spread of COVID-19. The presence of SARS-CoV-2 can bedetected by RT-PCR (it detects RNA of the virus) or by the presence of viral antigens inbiological fluids in ELISA or similar techniques using antibodies developed in animals.The aim of the study was the establishment of a quantitative polyclonal sera-based test forroutine measurement of the concentration of SARS CoV-2 nucleocapsid protein usingabsorbance measurement in a standard 96-well microtiter plate. For the purposes of the testdevelopment, recombinant N protein was produced and used for the production of miceand rabbit antisera. Produced antisera were purified and titer was determined. High-affinitypolyclonal N-protein specific antisera were used for N-protein specific ELISA testdevelopment. The test is based on mice polyclonal sera adhered to microtiter plate bottomfor the capture of the N protein from the specimen. Various concentrations of therecombinant N-protein were used to generate a standard curve for protein quantification.The N-protein bound to the mice antibodies was detected with rabbit polyclonal sera andanti-rabbit antibody coupled to an enzyme that provides spectrophotometric measurement.We have successfully developed the prototype ELISA for the quantification of N-proteinwith the detection limit being in the range of ng/mL. The average LOD value for theprototype ELISA was determined to be 9.2 ng/mL, while the average LOQ value was10.2 ng/mL. We have demonstrated that produced polyclonal antisera are suitable for thedetection of N-protein with affinity and specificity similar to, or better than commercialantibodies. Furthermore, the prototype ELISA can be used with satisfactory confidence forquantification of the N-protein in protein-rich samples, similar to human sera.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine",
title = "Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein, Development of SARS-CoV-2 N-protein specific capture ELISA",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5362"
}
Radomirović, M. Ž., Simović, A., Udovički, B. D., Krstić-Ristivojević, M. V., Sabljić, L. Z., Lukić, I. D., Glamočlija, S. Đ., Ćujić, D. R., Gnjatović, M. Lj., Stojanović, M. M., Stanić-Vučinić, D., Radosavljević, J.,& Ćirković-Veličković, T.. (2022). Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein. in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine
Beograd : Srpsko hemijsko društvo..
https://hdl.handle.net/21.15107/rcub_cherry_5362
Radomirović MŽ, Simović A, Udovički BD, Krstić-Ristivojević MV, Sabljić LZ, Lukić ID, Glamočlija SĐ, Ćujić DR, Gnjatović ML, Stojanović MM, Stanić-Vučinić D, Radosavljević J, Ćirković-Veličković T. Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein. in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine. 2022;.
https://hdl.handle.net/21.15107/rcub_cherry_5362 .
Radomirović, Mirjana Ž., Simović, Ana, Udovički, Božidar D., Krstić-Ristivojević, Maja V., Sabljić, Ljiljana Z., Lukić, Ivana D., Glamočlija, Sofija Đ., Ćujić, Danica R., Gnjatović, Marija Lj., Stojanović, Marijana M., Stanić-Vučinić, Dragana, Radosavljević, Jelena, Ćirković-Veličković, Tanja, "Razvoj sendvič ELISA testa specifičnog za SARS-CoV-2 N-protein" in 58. Savetovanje Srpskog hemijskog društva, Kratki izvodi radova, Beograd 9. i 10. jun 2022. godine (2022),
https://hdl.handle.net/21.15107/rcub_cherry_5362 .

Comparative profiling and exposure assessment of microplastics in differently sized Manila clams from South Korea by μFTIR and Nile Red staining

de Guzman, Maria Krishna; Anđelković, Mirjana; Jovanović, Vesna B.; Jung, Jaehak; Kim, Juyang; Dailey, Lea Ann; Rajković, Andreja; De Meulenaer, Bruno; Ćirković-Veličković, Tanja

(Elsevier, 2022)

TY  - JOUR
AU  - de Guzman, Maria Krishna
AU  - Anđelković, Mirjana
AU  - Jovanović, Vesna B.
AU  - Jung, Jaehak
AU  - Kim, Juyang
AU  - Dailey, Lea Ann
AU  - Rajković, Andreja
AU  - De Meulenaer, Bruno
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://hdl.handle.net/1854/LU-8759702
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5420
AB  - The accumulation of microplastics in marine organisms is an emerging concern. Due to trophic transfer, the
safety of seafood is under investigation in view of the potential negative effects of microplastics on human health.
In this study, market samples of Manila clams (Ruditapes philippinarum) from South Korea were segregated into
two groups of considerably different size (p < 0.05), namely small clams with shell length of 40.69 ± 3.97 mm,
and large clams of shell length 51.19 ± 2.86 mm. Comparative profiling of the number, size, shape, and polymer
type of microplastics were performed using μFTIR imaging and Nile red staining. Overall, μFTIR detected only
1559 microplastics while 1996 microplastics were counted based on staining from 61 Manila clams (30 small and
31 large), leading to an overestimation of 18 to 75 %. Comparable microplastics concentration, based on μFTIR,
were observed at 2.70 ± 1.66 MP/g or 15.64 ± 9.25 MP/individual for the small samples, and 3.65 ± 1.59 MP/g
or 41.63 ± 16.90 MP/individual for the large ones (p > 0.05). Particle diameters of 20–100 μm was the most
dominant, accounting for 44.6 % and 46.5 % of all microplastics from the small and large groups, respectively.
Particles, with a circularity (resemblance to a circle) value between 0.6 and 1.0, were the most prevalent, fol-
lowed by fragments and fibers. At least 50 % of microplastics from the small and large samples were polystyrene,
making it the most abundant polymer type. Despite the substantial difference in the size of the animals, only a
weak to moderate correlation was observed between microplastics content and the physical attributes of the
clams such as shell length and weight, (soft) tissue weight, and total weight (Spearman's coefficient < 0.5). The
estimated intake of microplastics by the Korean population was 1232 MP/person/year via small clams, 1663 MP/
person/year via large clams, and 1489 MP/person/year via clams independent of size.
PB  - Elsevier
T2  - Marine Pollution Bulletin
T1  - Comparative profiling and exposure assessment of microplastics in differently sized Manila clams from South Korea by μFTIR and Nile Red staining
VL  - 181
SP  - 113846
DO  - 10.1016/j.marpolbul.2022.113846
ER  - 
@article{
author = "de Guzman, Maria Krishna and Anđelković, Mirjana and Jovanović, Vesna B. and Jung, Jaehak and Kim, Juyang and Dailey, Lea Ann and Rajković, Andreja and De Meulenaer, Bruno and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "The accumulation of microplastics in marine organisms is an emerging concern. Due to trophic transfer, the
safety of seafood is under investigation in view of the potential negative effects of microplastics on human health.
In this study, market samples of Manila clams (Ruditapes philippinarum) from South Korea were segregated into
two groups of considerably different size (p < 0.05), namely small clams with shell length of 40.69 ± 3.97 mm,
and large clams of shell length 51.19 ± 2.86 mm. Comparative profiling of the number, size, shape, and polymer
type of microplastics were performed using μFTIR imaging and Nile red staining. Overall, μFTIR detected only
1559 microplastics while 1996 microplastics were counted based on staining from 61 Manila clams (30 small and
31 large), leading to an overestimation of 18 to 75 %. Comparable microplastics concentration, based on μFTIR,
were observed at 2.70 ± 1.66 MP/g or 15.64 ± 9.25 MP/individual for the small samples, and 3.65 ± 1.59 MP/g
or 41.63 ± 16.90 MP/individual for the large ones (p > 0.05). Particle diameters of 20–100 μm was the most
dominant, accounting for 44.6 % and 46.5 % of all microplastics from the small and large groups, respectively.
Particles, with a circularity (resemblance to a circle) value between 0.6 and 1.0, were the most prevalent, fol-
lowed by fragments and fibers. At least 50 % of microplastics from the small and large samples were polystyrene,
making it the most abundant polymer type. Despite the substantial difference in the size of the animals, only a
weak to moderate correlation was observed between microplastics content and the physical attributes of the
clams such as shell length and weight, (soft) tissue weight, and total weight (Spearman's coefficient < 0.5). The
estimated intake of microplastics by the Korean population was 1232 MP/person/year via small clams, 1663 MP/
person/year via large clams, and 1489 MP/person/year via clams independent of size.",
publisher = "Elsevier",
journal = "Marine Pollution Bulletin",
title = "Comparative profiling and exposure assessment of microplastics in differently sized Manila clams from South Korea by μFTIR and Nile Red staining",
volume = "181",
pages = "113846",
doi = "10.1016/j.marpolbul.2022.113846"
}
de Guzman, M. K., Anđelković, M., Jovanović, V. B., Jung, J., Kim, J., Dailey, L. A., Rajković, A., De Meulenaer, B.,& Ćirković-Veličković, T.. (2022). Comparative profiling and exposure assessment of microplastics in differently sized Manila clams from South Korea by μFTIR and Nile Red staining. in Marine Pollution Bulletin
Elsevier., 181, 113846.
https://doi.org/10.1016/j.marpolbul.2022.113846
de Guzman MK, Anđelković M, Jovanović VB, Jung J, Kim J, Dailey LA, Rajković A, De Meulenaer B, Ćirković-Veličković T. Comparative profiling and exposure assessment of microplastics in differently sized Manila clams from South Korea by μFTIR and Nile Red staining. in Marine Pollution Bulletin. 2022;181:113846.
doi:10.1016/j.marpolbul.2022.113846 .
de Guzman, Maria Krishna, Anđelković, Mirjana, Jovanović, Vesna B., Jung, Jaehak, Kim, Juyang, Dailey, Lea Ann, Rajković, Andreja, De Meulenaer, Bruno, Ćirković-Veličković, Tanja, "Comparative profiling and exposure assessment of microplastics in differently sized Manila clams from South Korea by μFTIR and Nile Red staining" in Marine Pollution Bulletin, 181 (2022):113846,
https://doi.org/10.1016/j.marpolbul.2022.113846 . .
3
2

Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting

Đukić, Teodora; Smiljanić, Katarina; Mihailović, Jelena; Prodić, Ivana; Apostolović, Danijela; Liu, Shu-Hua; Epstein, Michelle M.; van Hage, Marianne; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(MDPI, 2022)

TY  - JOUR
AU  - Đukić, Teodora
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Liu, Shu-Hua
AU  - Epstein, Michelle M.
AU  - van Hage, Marianne
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5702
AB  - Post-translational modifications (PTMs) are covalent changes occurring on amino acid side chains of proteins and yet are neglected structural and functional aspects of protein architecture. The objective was to detect differences in PTM profiles that take place after roasting using open PTM search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms of modification versatility and extent. The most frequent PTM was methionine oxidation, especially in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation (Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study provides a better understanding of how roasting impacts the PTM profile of major peanut allergens and provides a good foundation for further exploration of PTMs.
PB  - MDPI
T2  - Foods
T1  - Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting
VL  - 11
IS  - 24
EP  - 3993
DO  - 10.3390/foods11243993
ER  - 
@article{
author = "Đukić, Teodora and Smiljanić, Katarina and Mihailović, Jelena and Prodić, Ivana and Apostolović, Danijela and Liu, Shu-Hua and Epstein, Michelle M. and van Hage, Marianne and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Post-translational modifications (PTMs) are covalent changes occurring on amino acid side chains of proteins and yet are neglected structural and functional aspects of protein architecture. The objective was to detect differences in PTM profiles that take place after roasting using open PTM search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms of modification versatility and extent. The most frequent PTM was methionine oxidation, especially in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation (Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study provides a better understanding of how roasting impacts the PTM profile of major peanut allergens and provides a good foundation for further exploration of PTMs.",
publisher = "MDPI",
journal = "Foods",
title = "Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting",
volume = "11",
number = "24",
pages = "3993",
doi = "10.3390/foods11243993"
}
Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S., Epstein, M. M., van Hage, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. in Foods
MDPI., 11(24).
https://doi.org/10.3390/foods11243993
Đukić T, Smiljanić K, Mihailović J, Prodić I, Apostolović D, Liu S, Epstein MM, van Hage M, Stanić-Vučinić D, Ćirković-Veličković T. Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. in Foods. 2022;11(24):null-3993.
doi:10.3390/foods11243993 .
Đukić, Teodora, Smiljanić, Katarina, Mihailović, Jelena, Prodić, Ivana, Apostolović, Danijela, Liu, Shu-Hua, Epstein, Michelle M., van Hage, Marianne, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting" in Foods, 11, no. 24 (2022),
https://doi.org/10.3390/foods11243993 . .

Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993

Đukić, Teodora; Smiljanić, Katarina; Mihailović, Jelena; Prodić, Ivana; Apostolović, Danijela; Liu, Shu-Hua; Epstein, Michelle M.; van Hage, Marianne; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(MDPI, 2022)

TY  - DATA
AU  - Đukić, Teodora
AU  - Smiljanić, Katarina
AU  - Mihailović, Jelena
AU  - Prodić, Ivana
AU  - Apostolović, Danijela
AU  - Liu, Shu-Hua
AU  - Epstein, Michelle M.
AU  - van Hage, Marianne
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5708
AB  - Post-translational modifications (PTMs) are covalent changes occurring on amino acid side chains of proteins and yet are neglected structural and functional aspects of protein architecture. The objective was to detect differences in PTM profiles that take place after roasting using open PTM search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms of modification versatility and extent. The most frequent PTM was methionine oxidation, especially in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation (Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study provides a better understanding of how roasting impacts the PTM profile of major peanut allergens and provides a good foundation for further exploration of PTMs.
PB  - MDPI
T2  - Foods
T1  - Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993
VL  - 11
IS  - 24
EP  - 3993
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5708
ER  - 
@misc{
author = "Đukić, Teodora and Smiljanić, Katarina and Mihailović, Jelena and Prodić, Ivana and Apostolović, Danijela and Liu, Shu-Hua and Epstein, Michelle M. and van Hage, Marianne and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Post-translational modifications (PTMs) are covalent changes occurring on amino acid side chains of proteins and yet are neglected structural and functional aspects of protein architecture. The objective was to detect differences in PTM profiles that take place after roasting using open PTM search. We conducted a bottom-up proteomic study to investigate the impact of peanut roasting on readily soluble allergens and their PTM profiles. Proteomic PTM profiling of certain modifications was confirmed by Western blotting with a series of PTM-specific antibodies. In addition to inducing protein aggregation and denaturation, roasting may facilitate change in their PTM pattern and relative profiling. We have shown that Ara h 1 is the most modified major allergen in both samples in terms of modification versatility and extent. The most frequent PTM was methionine oxidation, especially in roasted samples. PTMs uniquely found in roasted samples were hydroxylation (Trp), formylation (Arg/Lys), and oxidation or hydroxylation (Asn). Raw and roasted peanut extracts did not differ in the binding of IgE from the serum of peanut-sensitised individuals done by ELISA. This study provides a better understanding of how roasting impacts the PTM profile of major peanut allergens and provides a good foundation for further exploration of PTMs.",
publisher = "MDPI",
journal = "Foods",
title = "Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993",
volume = "11",
number = "24",
pages = "3993",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5708"
}
Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S., Epstein, M. M., van Hage, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2022). Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993. in Foods
MDPI., 11(24).
https://hdl.handle.net/21.15107/rcub_cherry_5708
Đukić T, Smiljanić K, Mihailović J, Prodić I, Apostolović D, Liu S, Epstein MM, van Hage M, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993. in Foods. 2022;11(24):null-3993.
https://hdl.handle.net/21.15107/rcub_cherry_5708 .
Đukić, Teodora, Smiljanić, Katarina, Mihailović, Jelena, Prodić, Ivana, Apostolović, Danijela, Liu, Shu-Hua, Epstein, Michelle M., van Hage, Marianne, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Supplementary for: Đukić, T., Smiljanić, K., Mihailović, J., Prodić, I., Apostolović, D., Liu, S.-H., Epstein, M. M., van Hage, M., Stanić-Vučinić, D., & Ćirković Veličković, T. (2022). Proteomic Profiling of Major Peanut Allergens and Their Post-Translational Modifications Affected by Roasting. Foods, 11(24). https://doi.org/10.3390/foods11243993" in Foods, 11, no. 24 (2022),
https://hdl.handle.net/21.15107/rcub_cherry_5708 .

MP-Net: Deep learning-based segmentation for fluorescence microscopy images of microplastics isolated from clams

Ćirković-Veličković, Tanja; Park, Ho-Min; de Guzman, Maria Krishna; de Neve, Wesley; Van Messem, Arnout; Baek, Ji Yeon; Park, Sanghyeon

(Public Library of Science, 2022)

TY  - JOUR
AU  - Ćirković-Veličković, Tanja
AU  - Park, Ho-Min
AU  - de Guzman, Maria Krishna
AU  - de Neve, Wesley
AU  - Van Messem, Arnout
AU  - Baek, Ji Yeon
AU  - Park, Sanghyeon
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5733
AB  - Environmental monitoring of microplastics (MP) contamination has become an area of great research interest, given potential hazards associated with human ingestion of MP. In this context, determination of MP concentration is essential. However, cheap, rapid, and accurate quantification of MP remains a challenge to this date. This study proposes a deep learning-based image segmentation method that properly distinguishes fluorescent MP from other elements in a given microscopy image. A total of nine different deep learning models, six of which are based on U-Net, were investigated. These models were trained using at least 20,000 patches sampled from 99 fluorescence microscopy images of MP and their corresponding binary masks. MP-Net, which is derived from U-Net, was found to be the best performing model, exhibiting the highest mean F1-score (0.736) and mean IoU value (0.617). Test-time augmentation (using brightness, contrast, and HSV) was applied to MP-Net for robust learning. However, compared to the results obtained without augmentation, no clear improvement in predictive performance could be observed. Recovery assessment for both spiked and real images showed that, compared to already existing tools for MP quantification, the MP quantities predicted by MP-Net are those closest to the ground truth. This observation suggests that MP-Net allows creating masks that more accurately reflect the quantitative presence of fluorescent MP in microscopy images. Finally, MAP (Microplastics Annotation Package) is introduced, an integrated software environment for automated MP quantification, offering support for MP-Net, already existing MP analysis tools like MP-VAT, manual annotation, and model fine-tuning.
PB  - Public Library of Science
T2  - PLoS ONE
T1  - MP-Net: Deep learning-based segmentation for fluorescence microscopy images of microplastics isolated from clams
VL  - 17
IS  - 6
SP  - e0269449
DO  - 10.1371/journal.pone.0269449
ER  - 
@article{
author = "Ćirković-Veličković, Tanja and Park, Ho-Min and de Guzman, Maria Krishna and de Neve, Wesley and Van Messem, Arnout and Baek, Ji Yeon and Park, Sanghyeon",
year = "2022",
abstract = "Environmental monitoring of microplastics (MP) contamination has become an area of great research interest, given potential hazards associated with human ingestion of MP. In this context, determination of MP concentration is essential. However, cheap, rapid, and accurate quantification of MP remains a challenge to this date. This study proposes a deep learning-based image segmentation method that properly distinguishes fluorescent MP from other elements in a given microscopy image. A total of nine different deep learning models, six of which are based on U-Net, were investigated. These models were trained using at least 20,000 patches sampled from 99 fluorescence microscopy images of MP and their corresponding binary masks. MP-Net, which is derived from U-Net, was found to be the best performing model, exhibiting the highest mean F1-score (0.736) and mean IoU value (0.617). Test-time augmentation (using brightness, contrast, and HSV) was applied to MP-Net for robust learning. However, compared to the results obtained without augmentation, no clear improvement in predictive performance could be observed. Recovery assessment for both spiked and real images showed that, compared to already existing tools for MP quantification, the MP quantities predicted by MP-Net are those closest to the ground truth. This observation suggests that MP-Net allows creating masks that more accurately reflect the quantitative presence of fluorescent MP in microscopy images. Finally, MAP (Microplastics Annotation Package) is introduced, an integrated software environment for automated MP quantification, offering support for MP-Net, already existing MP analysis tools like MP-VAT, manual annotation, and model fine-tuning.",
publisher = "Public Library of Science",
journal = "PLoS ONE",
title = "MP-Net: Deep learning-based segmentation for fluorescence microscopy images of microplastics isolated from clams",
volume = "17",
number = "6",
pages = "e0269449",
doi = "10.1371/journal.pone.0269449"
}
Ćirković-Veličković, T., Park, H., de Guzman, M. K., de Neve, W., Van Messem, A., Baek, J. Y.,& Park, S.. (2022). MP-Net: Deep learning-based segmentation for fluorescence microscopy images of microplastics isolated from clams. in PLoS ONE
Public Library of Science., 17(6), e0269449.
https://doi.org/10.1371/journal.pone.0269449
Ćirković-Veličković T, Park H, de Guzman MK, de Neve W, Van Messem A, Baek JY, Park S. MP-Net: Deep learning-based segmentation for fluorescence microscopy images of microplastics isolated from clams. in PLoS ONE. 2022;17(6):e0269449.
doi:10.1371/journal.pone.0269449 .
Ćirković-Veličković, Tanja, Park, Ho-Min, de Guzman, Maria Krishna, de Neve, Wesley, Van Messem, Arnout, Baek, Ji Yeon, Park, Sanghyeon, "MP-Net: Deep learning-based segmentation for fluorescence microscopy images of microplastics isolated from clams" in PLoS ONE, 17, no. 6 (2022):e0269449,
https://doi.org/10.1371/journal.pone.0269449 . .
2
1

Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk

Radosavljević, Jelena; Stanić-Vučinić, Dragana; Stojadinović, Marija M.; Radomirović, Mirjana Ž.; Simović, Ana; Radibratović, Milica; Ćirković-Veličković, Tanja

(Bentham Science, 2022)

TY  - JOUR
AU  - Radosavljević, Jelena
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Radomirović, Mirjana Ž.
AU  - Simović, Ana
AU  - Radibratović, Milica
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4883
AB  - Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.
PB  - Bentham Science
T2  - Current Analytical Chemistry
T1  - Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk
VL  - 18
IS  - 3
SP  - 341
EP  - 359
DO  - 10.2174/1573411017666210108092338
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4883
ER  - 
@article{
author = "Radosavljević, Jelena and Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Radomirović, Mirjana Ž. and Simović, Ana and Radibratović, Milica and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.",
publisher = "Bentham Science",
journal = "Current Analytical Chemistry",
title = "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk",
volume = "18",
number = "3",
pages = "341-359",
doi = "10.2174/1573411017666210108092338",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4883"
}
Radosavljević, J., Stanić-Vučinić, D., Stojadinović, M. M., Radomirović, M. Ž., Simović, A., Radibratović, M.,& Ćirković-Veličković, T.. (2022). Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry
Bentham Science., 18(3), 341-359.
https://doi.org/10.2174/1573411017666210108092338
https://hdl.handle.net/21.15107/rcub_cherry_4883
Radosavljević J, Stanić-Vučinić D, Stojadinović MM, Radomirović MŽ, Simović A, Radibratović M, Ćirković-Veličković T. Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry. 2022;18(3):341-359.
doi:10.2174/1573411017666210108092338
https://hdl.handle.net/21.15107/rcub_cherry_4883 .
Radosavljević, Jelena, Stanić-Vučinić, Dragana, Stojadinović, Marija M., Radomirović, Mirjana Ž., Simović, Ana, Radibratović, Milica, Ćirković-Veličković, Tanja, "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk" in Current Analytical Chemistry, 18, no. 3 (2022):341-359,
https://doi.org/10.2174/1573411017666210108092338 .,
https://hdl.handle.net/21.15107/rcub_cherry_4883 .
2
1
1

Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk

Stanić-Vučinić, Dragana; Stojadinović, Marija M.; Radomirović, Mirjana Ž.; Simović, Ana; Radibratović, Milica; Ćirković-Veličković, Tanja

(Bentham Science, 2022)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Radomirović, Mirjana Ž.
AU  - Simović, Ana
AU  - Radibratović, Milica
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4884
AB  - Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.
PB  - Bentham Science
T2  - Current Analytical Chemistry
T1  - Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk
VL  - 18
IS  - 3
SP  - 341
EP  - 359
DO  - 10.2174/1573411017666210108092338
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4884
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Radomirović, Mirjana Ž. and Simović, Ana and Radibratović, Milica and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Background: The world’s production of whey is estimated to be more than 200 milliontons per year. Although whey is an important source of proteins with high nutritional value andbiotechnological importance, it is still considered as a by-product of the dairy industry with loweconomic value due to low industrial exploitation. There are several challenges in the separation ofwhey proteins: low concentration, the complexity of the material and similar properties (pI, molecularmass) of some proteins.Methods: A narrative review of all the relevant papers on the present methodologies based on ionexchange and adsorption principles for isolation of whey proteins, known to the authors, was conductedResults: Traditional ion exchange techniques are widely used for the separation and purification ofthe bovine whey proteins. These methodologies, based on the anion or cation chromatographicprocedures, as well as the combination of aforementioned techniques are still preferential methodsfor the isolation of the whey proteins on the laboratory scale. However, more recent research on ionexchange membranes for this purpose has been introduced, with promising potential to be appliedon the pilot industrial scale. Newly developed methodologies based either on the ion exchangeseparation (for example: simulated moving bed chromatography, expanded bed adsorption, magneticion exchangers, etc.) or adsorption (for example: adsorption on hydroxyapatite or activatedcarbon, or molecular imprinting) are promising approaches for scaling up of the whey proteins’purification processes.Conclusion: Many procedures based on ion exchange are successfully implemented for the separationand purification of whey proteins, providing protein preparations of moderate-to-high yieldand satisfactory purity. However, the authors anticipate further development of adsorption-basedmethodologies for the separation of whey proteins by targeting the differences in proteins’ structuresrather than targeting the differences in molecular masses and pI. The complex composite multilayeredmatrices, including also inorganic components, are promising materials for simultaneousexploiting of the differences in the masses, pI and structures of whey proteins for the separation.",
publisher = "Bentham Science",
journal = "Current Analytical Chemistry",
title = "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk",
volume = "18",
number = "3",
pages = "341-359",
doi = "10.2174/1573411017666210108092338",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4884"
}
Stanić-Vučinić, D., Stojadinović, M. M., Radomirović, M. Ž., Simović, A., Radibratović, M.,& Ćirković-Veličković, T.. (2022). Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry
Bentham Science., 18(3), 341-359.
https://doi.org/10.2174/1573411017666210108092338
https://hdl.handle.net/21.15107/rcub_cherry_4884
Stanić-Vučinić D, Stojadinović MM, Radomirović MŽ, Simović A, Radibratović M, Ćirković-Veličković T. Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk. in Current Analytical Chemistry. 2022;18(3):341-359.
doi:10.2174/1573411017666210108092338
https://hdl.handle.net/21.15107/rcub_cherry_4884 .
Stanić-Vučinić, Dragana, Stojadinović, Marija M., Radomirović, Mirjana Ž., Simović, Ana, Radibratović, Milica, Ćirković-Veličković, Tanja, "Application of Ion Exchange and Adsorption Techniques for Separation of Whey Proteins from Bovine Milk" in Current Analytical Chemistry, 18, no. 3 (2022):341-359,
https://doi.org/10.2174/1573411017666210108092338 .,
https://hdl.handle.net/21.15107/rcub_cherry_4884 .
2
1
1

Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes

Simović, Ana; Combet, Sophie; Ćirković-Veličković, Tanja; Nikolic, Milan; Minic, Simeon

(Sociedade Portuguesa de Química, 2022)

TY  - CONF
AU  - Simović, Ana
AU  - Combet, Sophie
AU  - Ćirković-Veličković, Tanja
AU  - Nikolic, Milan
AU  - Minic, Simeon
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5133
AB  - The high content of vitamins, minerals, antioxidants, and proteins makes red algae Porphyra sp. (Nori) superfood with exceptional health-promoting benefits. Its intense colour originates from R-phycoerythrin (R-PE), phycobiliprotein containing covalently attached tetrapyrrole chromophores: red phycoerythrobilin and orange phycourobilin. The present study aims to characterize the stability of R-PE, a natural colourant with a high potential for application in the food, cosmetic, and pharmaceutical industries. We purified R-PE from dried Nori flakes with a high purity ratio (A560 /A280 ≥5). Far-UV CD spectroscopic showed that α-helix is the dominant secondary structure (75%). The thermal unfolding of α-helix revealed two transitions (Tm1 and Tm2 at 56 and 72°C, respectively), ascribed to the different subunits of R-PE. Absorption measurements showed that high pressure (HP) induces dissociation of R-PE into subunits followed by subunit unfolding. Contrary to temperature, HP treatment showed a significant advantage under applied conditions: the protein unfolding is partly reversible, and the R-PE colour bleaching is minimized. Based on the fluorescence quenching approach, R-PE's binding affinities for Cu2+ and Zn2+ ions were 6.27x105 and 1.71x103 M-1, respectively. Absorption and near-UV/VIS CD spectroscopy suggested conformational changes in protein chromophores upon metal ions binding. Far-UV CD spectroscopy did not reveal that metal binding affects R-PE structure. The obtained results give new insights into the stability of R-PE with a good use-value in replacement of toxic synthetic dyes, preservation of R-PE red colour in fortified food and beverages by HP processing, and as a biosensor for Cu2+ in aquatic life systems.
Acknowledgments: This study was financially supported by the Ministry of Education, Science and Technological Development of the Republic of Serbia, Contract number: 451-03-9/2021-14/200168 and the European Commission, under the Horizon2020, FoodEnTwin Project, GA No. 810752.
PB  - Sociedade Portuguesa de Química
C3  - Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference
T1  - Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes
SP  - 138
EP  - 138
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5133
ER  - 
@conference{
author = "Simović, Ana and Combet, Sophie and Ćirković-Veličković, Tanja and Nikolic, Milan and Minic, Simeon",
year = "2022",
abstract = "The high content of vitamins, minerals, antioxidants, and proteins makes red algae Porphyra sp. (Nori) superfood with exceptional health-promoting benefits. Its intense colour originates from R-phycoerythrin (R-PE), phycobiliprotein containing covalently attached tetrapyrrole chromophores: red phycoerythrobilin and orange phycourobilin. The present study aims to characterize the stability of R-PE, a natural colourant with a high potential for application in the food, cosmetic, and pharmaceutical industries. We purified R-PE from dried Nori flakes with a high purity ratio (A560 /A280 ≥5). Far-UV CD spectroscopic showed that α-helix is the dominant secondary structure (75%). The thermal unfolding of α-helix revealed two transitions (Tm1 and Tm2 at 56 and 72°C, respectively), ascribed to the different subunits of R-PE. Absorption measurements showed that high pressure (HP) induces dissociation of R-PE into subunits followed by subunit unfolding. Contrary to temperature, HP treatment showed a significant advantage under applied conditions: the protein unfolding is partly reversible, and the R-PE colour bleaching is minimized. Based on the fluorescence quenching approach, R-PE's binding affinities for Cu2+ and Zn2+ ions were 6.27x105 and 1.71x103 M-1, respectively. Absorption and near-UV/VIS CD spectroscopy suggested conformational changes in protein chromophores upon metal ions binding. Far-UV CD spectroscopy did not reveal that metal binding affects R-PE structure. The obtained results give new insights into the stability of R-PE with a good use-value in replacement of toxic synthetic dyes, preservation of R-PE red colour in fortified food and beverages by HP processing, and as a biosensor for Cu2+ in aquatic life systems.
Acknowledgments: This study was financially supported by the Ministry of Education, Science and Technological Development of the Republic of Serbia, Contract number: 451-03-9/2021-14/200168 and the European Commission, under the Horizon2020, FoodEnTwin Project, GA No. 810752.",
publisher = "Sociedade Portuguesa de Química",
journal = "Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference",
title = "Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes",
pages = "138-138",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5133"
}
Simović, A., Combet, S., Ćirković-Veličković, T., Nikolic, M.,& Minic, S.. (2022). Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes. in Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference
Sociedade Portuguesa de Química., 138-138.
https://hdl.handle.net/21.15107/rcub_cherry_5133
Simović A, Combet S, Ćirković-Veličković T, Nikolic M, Minic S. Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes. in Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference. 2022;:138-138.
https://hdl.handle.net/21.15107/rcub_cherry_5133 .
Simović, Ana, Combet, Sophie, Ćirković-Veličković, Tanja, Nikolic, Milan, Minic, Simeon, "Probing the stability of the food colourant R-phycoerythrin from dried Nori flakes" in Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference (2022):138-138,
https://hdl.handle.net/21.15107/rcub_cherry_5133 .

Microplastics in food: scoping review on health effects, occurrence, and human exposure

Udovički, Božidar; Anđelković, Mirjana; Ćirković-Veličković, Tanja; Rajković, Andreja

(BMC, 2022)

TY  - JOUR
AU  - Udovički, Božidar
AU  - Anđelković, Mirjana
AU  - Ćirković-Veličković, Tanja
AU  - Rajković, Andreja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5509
AB  - With most of the plastics ever produced now being waste, slowly degrading and fragmenting in the environment, microplastics (MPs) have become an emerging concern regarding their presence in food and influence on human health. While many studies on marine ecotoxicology and the occurrence of MPs in fish and shellfish exist, research on the occurrence of MPs in other foods and their effect on human health is still in early-stage, but the attention is increasing. This review aimed to provide relevant information on the possible health effect of ingested MPs, the occurrence, and levels of MPs contamination in various foods and estimated exposure to MPs through food. Potential toxic consequences from exposure to MPs through food can arise from MPs themselves, diffused monomers and additives but also from sorbed contaminants or microorganisms that colonise MPs. Recent publications have confirmed widespread contamination of our food with MPs including basic and life-essential constituents such as water and salt providing the basis for chronic exposure. Available exposure assessments indicate that we ingest up to several hundred thousand MPs particles yearly.
PB  - BMC
T2  - International Journal of Food Contamination
T1  - Microplastics in food: scoping review on health effects, occurrence, and human exposure
VL  - 9
IS  - 1
DO  - 10.1186/s40550-022-00093-6
ER  - 
@article{
author = "Udovički, Božidar and Anđelković, Mirjana and Ćirković-Veličković, Tanja and Rajković, Andreja",
year = "2022",
abstract = "With most of the plastics ever produced now being waste, slowly degrading and fragmenting in the environment, microplastics (MPs) have become an emerging concern regarding their presence in food and influence on human health. While many studies on marine ecotoxicology and the occurrence of MPs in fish and shellfish exist, research on the occurrence of MPs in other foods and their effect on human health is still in early-stage, but the attention is increasing. This review aimed to provide relevant information on the possible health effect of ingested MPs, the occurrence, and levels of MPs contamination in various foods and estimated exposure to MPs through food. Potential toxic consequences from exposure to MPs through food can arise from MPs themselves, diffused monomers and additives but also from sorbed contaminants or microorganisms that colonise MPs. Recent publications have confirmed widespread contamination of our food with MPs including basic and life-essential constituents such as water and salt providing the basis for chronic exposure. Available exposure assessments indicate that we ingest up to several hundred thousand MPs particles yearly.",
publisher = "BMC",
journal = "International Journal of Food Contamination",
title = "Microplastics in food: scoping review on health effects, occurrence, and human exposure",
volume = "9",
number = "1",
doi = "10.1186/s40550-022-00093-6"
}
Udovički, B., Anđelković, M., Ćirković-Veličković, T.,& Rajković, A.. (2022). Microplastics in food: scoping review on health effects, occurrence, and human exposure. in International Journal of Food Contamination
BMC., 9(1).
https://doi.org/10.1186/s40550-022-00093-6
Udovički B, Anđelković M, Ćirković-Veličković T, Rajković A. Microplastics in food: scoping review on health effects, occurrence, and human exposure. in International Journal of Food Contamination. 2022;9(1).
doi:10.1186/s40550-022-00093-6 .
Udovički, Božidar, Anđelković, Mirjana, Ćirković-Veličković, Tanja, Rajković, Andreja, "Microplastics in food: scoping review on health effects, occurrence, and human exposure" in International Journal of Food Contamination, 9, no. 1 (2022),
https://doi.org/10.1186/s40550-022-00093-6 . .
6
5

INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity

Prodić, Ivana; Smiljanić, Katarina; Nagl, Christoph; Ballmer-Weber, Barbara; Hoffmann-Sommergruber, Karin; Ćirković-Veličković, Tanja

(MDPI, 2022)

TY  - JOUR
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Nagl, Christoph
AU  - Ballmer-Weber, Barbara
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5653
AB  - Most of the food allergens sensitized via the gastrointestinal tract resist thermal treatments and digestion, particularly digestion by pepsin. Roasted hazelnuts are more commonly consumed than raw ones. Since no studies have characterized gastric digestion protein fragments of raw and roasted hazelnuts nor their IgE binding properties, we compared these aspects of raw and roasted hazelnuts’ gastric digesta obtained by INFOGEST protocol. Their electrophoretically resolved profiles were probed with hazelnut allergic patients’ sera in 1D and 2D immunoblots. Electrophoretic profiles demonstrated pepsin digestion of all hazelnut allergens to varying extents. While 2D immunoblots indicated that roasting slightly reduced allergenicity, IgE ELISA with the pool of sera showed a slight significant (10%) increase in IgE binding in both gastric digesta. Cor a 9 isolated from the raw and roasted hazelnuts, characterized by far and near CD, remained stable after roasting, with preserved IgE reactivity. Its immunoreactivity contribution by inhibitory ELISA was noticeable in raw and roasted hazelnut digesta; its activity was slightly stronger in the roasted preparations. Roasting has a visible impact on proteins; however, it did not affect overall IgE reactivity. Gastric digestion slightly increases the overall IgE reactivity in raw and roasted hazelnuts, and may therefore impact the profiles of allergens and their fragments available to interact with the immune system in the small intestine. © 2022 by the authors.
PB  - MDPI
T2  - Foods
T1  - INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity
VL  - 11
SP  - 2914
DO  - 10.3390/foods11182914
ER  - 
@article{
author = "Prodić, Ivana and Smiljanić, Katarina and Nagl, Christoph and Ballmer-Weber, Barbara and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Most of the food allergens sensitized via the gastrointestinal tract resist thermal treatments and digestion, particularly digestion by pepsin. Roasted hazelnuts are more commonly consumed than raw ones. Since no studies have characterized gastric digestion protein fragments of raw and roasted hazelnuts nor their IgE binding properties, we compared these aspects of raw and roasted hazelnuts’ gastric digesta obtained by INFOGEST protocol. Their electrophoretically resolved profiles were probed with hazelnut allergic patients’ sera in 1D and 2D immunoblots. Electrophoretic profiles demonstrated pepsin digestion of all hazelnut allergens to varying extents. While 2D immunoblots indicated that roasting slightly reduced allergenicity, IgE ELISA with the pool of sera showed a slight significant (10%) increase in IgE binding in both gastric digesta. Cor a 9 isolated from the raw and roasted hazelnuts, characterized by far and near CD, remained stable after roasting, with preserved IgE reactivity. Its immunoreactivity contribution by inhibitory ELISA was noticeable in raw and roasted hazelnut digesta; its activity was slightly stronger in the roasted preparations. Roasting has a visible impact on proteins; however, it did not affect overall IgE reactivity. Gastric digestion slightly increases the overall IgE reactivity in raw and roasted hazelnuts, and may therefore impact the profiles of allergens and their fragments available to interact with the immune system in the small intestine. © 2022 by the authors.",
publisher = "MDPI",
journal = "Foods",
title = "INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity",
volume = "11",
pages = "2914",
doi = "10.3390/foods11182914"
}
Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods
MDPI., 11, 2914.
https://doi.org/10.3390/foods11182914
Prodić I, Smiljanić K, Nagl C, Ballmer-Weber B, Hoffmann-Sommergruber K, Ćirković-Veličković T. INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods. 2022;11:2914.
doi:10.3390/foods11182914 .
Prodić, Ivana, Smiljanić, Katarina, Nagl, Christoph, Ballmer-Weber, Barbara, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity" in Foods, 11 (2022):2914,
https://doi.org/10.3390/foods11182914 . .

Supplementary material for:Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods MDPI., 11, 2914. https://doi.org/10.3390/foods11182914

Prodić, Ivana; Smiljanić, Katarina; Nagl, Christoph; Ballmer-Weber, Barbara; Hoffmann-Sommergruber, Karin; Ćirković-Veličković, Tanja

(MDPI, 2022)

TY  - DATA
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Nagl, Christoph
AU  - Ballmer-Weber, Barbara
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2022
UR  - https://doi.org/10.3390/foods11182914
AB  - Most of the food allergens sensitized via the gastrointestinal tract resist thermal treatments and digestion, particularly digestion by pepsin. Roasted hazelnuts are more commonly consumed than raw ones. Since no studies have characterized gastric digestion protein fragments of raw and roasted hazelnuts nor their IgE binding properties, we compared these aspects of raw and roasted hazelnuts’ gastric digesta obtained by INFOGEST protocol. Their electrophoretically resolved profiles were probed with hazelnut allergic patients’ sera in 1D and 2D immunoblots. Electrophoretic profiles demonstrated pepsin digestion of all hazelnut allergens to varying extents. While 2D immunoblots indicated that roasting slightly reduced allergenicity, IgE ELISA with the pool of sera showed a slight significant (10%) increase in IgE binding in both gastric digesta. Cor a 9 isolated from the raw and roasted hazelnuts, characterized by far and near CD, remained stable after roasting, with preserved IgE reactivity. Its immunoreactivity contribution by inhibitory ELISA was noticeable in raw and roasted hazelnut digesta; its activity was slightly stronger in the roasted preparations. Roasting has a visible impact on proteins; however, it did not affect overall IgE reactivity. Gastric digestion slightly increases the overall IgE reactivity in raw and roasted hazelnuts, and may therefore impact the profiles of allergens and their fragments available to interact with the immune system in the small intestine. © 2022 by the authors.
PB  - MDPI
T2  - Foods
T1  - Supplementary material for:Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods MDPI., 11, 2914. https://doi.org/10.3390/foods11182914
VL  - 11
SP  - 2914
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5657
ER  - 
@misc{
author = "Prodić, Ivana and Smiljanić, Katarina and Nagl, Christoph and Ballmer-Weber, Barbara and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2022",
abstract = "Most of the food allergens sensitized via the gastrointestinal tract resist thermal treatments and digestion, particularly digestion by pepsin. Roasted hazelnuts are more commonly consumed than raw ones. Since no studies have characterized gastric digestion protein fragments of raw and roasted hazelnuts nor their IgE binding properties, we compared these aspects of raw and roasted hazelnuts’ gastric digesta obtained by INFOGEST protocol. Their electrophoretically resolved profiles were probed with hazelnut allergic patients’ sera in 1D and 2D immunoblots. Electrophoretic profiles demonstrated pepsin digestion of all hazelnut allergens to varying extents. While 2D immunoblots indicated that roasting slightly reduced allergenicity, IgE ELISA with the pool of sera showed a slight significant (10%) increase in IgE binding in both gastric digesta. Cor a 9 isolated from the raw and roasted hazelnuts, characterized by far and near CD, remained stable after roasting, with preserved IgE reactivity. Its immunoreactivity contribution by inhibitory ELISA was noticeable in raw and roasted hazelnut digesta; its activity was slightly stronger in the roasted preparations. Roasting has a visible impact on proteins; however, it did not affect overall IgE reactivity. Gastric digestion slightly increases the overall IgE reactivity in raw and roasted hazelnuts, and may therefore impact the profiles of allergens and their fragments available to interact with the immune system in the small intestine. © 2022 by the authors.",
publisher = "MDPI",
journal = "Foods",
title = "Supplementary material for:Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods MDPI., 11, 2914. https://doi.org/10.3390/foods11182914",
volume = "11",
pages = "2914",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5657"
}
Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). Supplementary material for:Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods MDPI., 11, 2914. https://doi.org/10.3390/foods11182914. in Foods
MDPI., 11, 2914.
https://hdl.handle.net/21.15107/rcub_cherry_5657
Prodić I, Smiljanić K, Nagl C, Ballmer-Weber B, Hoffmann-Sommergruber K, Ćirković-Veličković T. Supplementary material for:Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods MDPI., 11, 2914. https://doi.org/10.3390/foods11182914. in Foods. 2022;11:2914.
https://hdl.handle.net/21.15107/rcub_cherry_5657 .
Prodić, Ivana, Smiljanić, Katarina, Nagl, Christoph, Ballmer-Weber, Barbara, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Supplementary material for:Prodić, I., Smiljanić, K., Nagl, C., Ballmer-Weber, B., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2022). INFOGEST Digestion Assay of Raw and Roasted Hazelnuts and Its Impact on Allergens and Their IgE Binding Activity. in Foods MDPI., 11, 2914. https://doi.org/10.3390/foods11182914" in Foods, 11 (2022):2914,
https://hdl.handle.net/21.15107/rcub_cherry_5657 .

New applications of advanced instrumental techniques for the characterization of food allergenic proteins

Benedé, Sara; Lozano-Ojalvo, Daniel; Cristobal, Susana; Costa, Joana; D’Auria, Enza; Ćirković-Veličković, Tanja; Garrido-Arandia, María; Karakaya, Sibel; Mafra, Isabel; Mazzucchelli, Gabriel; Picariello, Gianluca; Romero-Sahagun, Alejandro; Villa, Caterina; Roncada, Paola; Molina, Elena

(Taylor & Francis Group, 2022)

TY  - JOUR
AU  - Benedé, Sara
AU  - Lozano-Ojalvo, Daniel
AU  - Cristobal, Susana
AU  - Costa, Joana
AU  - D’Auria, Enza
AU  - Ćirković-Veličković, Tanja
AU  - Garrido-Arandia, María
AU  - Karakaya, Sibel
AU  - Mafra, Isabel
AU  - Mazzucchelli, Gabriel
AU  - Picariello, Gianluca
AU  - Romero-Sahagun, Alejandro
AU  - Villa, Caterina
AU  - Roncada, Paola
AU  - Molina, Elena
PY  - 2022
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4548
AB  - Current approaches based on electrophoretic, chromatographic or immunochemical principles have allowed characterizing multiple allergens, mapping their epitopes, studying their mechanisms of action, developing detection and diagnostic methods and therapeutic strategies for the food and pharmaceutical industry. However, some of the common structural features related to the allergenic potential of food proteins remain unknown, or the pathological mechanism of food allergy is not yet fully understood. In addition, it is also necessary to evaluate new allergens from novel protein sources that may pose a new risk for consumers. Technological development has allowed the expansion of advanced technologies for which their whole potential has not been entirely exploited and could provide novel contributions to still unexplored molecular traits underlying both the structure of food allergens and the mechanisms through which they sensitize or elicit adverse responses in human subjects, as well as improving analytical techniques for their detection. This review presents cutting-edge instrumental techniques recently applied when studying structural and functional aspects of proteins, mechanism of action and interaction between biomolecules. We also exemplify their role in the food allergy research and discuss their new possible applications in several areas of the food allergy field.
PB  - Taylor & Francis Group
T2  - Critical Reviews in Food Science and Nutrition
T1  - New applications of advanced instrumental techniques for the characterization of food allergenic proteins
VL  - 62
IS  - 31
DO  - 10.1080/10408398.2021.1931806
ER  - 
@article{
author = "Benedé, Sara and Lozano-Ojalvo, Daniel and Cristobal, Susana and Costa, Joana and D’Auria, Enza and Ćirković-Veličković, Tanja and Garrido-Arandia, María and Karakaya, Sibel and Mafra, Isabel and Mazzucchelli, Gabriel and Picariello, Gianluca and Romero-Sahagun, Alejandro and Villa, Caterina and Roncada, Paola and Molina, Elena",
year = "2022",
abstract = "Current approaches based on electrophoretic, chromatographic or immunochemical principles have allowed characterizing multiple allergens, mapping their epitopes, studying their mechanisms of action, developing detection and diagnostic methods and therapeutic strategies for the food and pharmaceutical industry. However, some of the common structural features related to the allergenic potential of food proteins remain unknown, or the pathological mechanism of food allergy is not yet fully understood. In addition, it is also necessary to evaluate new allergens from novel protein sources that may pose a new risk for consumers. Technological development has allowed the expansion of advanced technologies for which their whole potential has not been entirely exploited and could provide novel contributions to still unexplored molecular traits underlying both the structure of food allergens and the mechanisms through which they sensitize or elicit adverse responses in human subjects, as well as improving analytical techniques for their detection. This review presents cutting-edge instrumental techniques recently applied when studying structural and functional aspects of proteins, mechanism of action and interaction between biomolecules. We also exemplify their role in the food allergy research and discuss their new possible applications in several areas of the food allergy field.",
publisher = "Taylor & Francis Group",
journal = "Critical Reviews in Food Science and Nutrition",
title = "New applications of advanced instrumental techniques for the characterization of food allergenic proteins",
volume = "62",
number = "31",
doi = "10.1080/10408398.2021.1931806"
}
Benedé, S., Lozano-Ojalvo, D., Cristobal, S., Costa, J., D’Auria, E., Ćirković-Veličković, T., Garrido-Arandia, M., Karakaya, S., Mafra, I., Mazzucchelli, G., Picariello, G., Romero-Sahagun, A., Villa, C., Roncada, P.,& Molina, E.. (2022). New applications of advanced instrumental techniques for the characterization of food allergenic proteins. in Critical Reviews in Food Science and Nutrition
Taylor & Francis Group., 62(31).
https://doi.org/10.1080/10408398.2021.1931806
Benedé S, Lozano-Ojalvo D, Cristobal S, Costa J, D’Auria E, Ćirković-Veličković T, Garrido-Arandia M, Karakaya S, Mafra I, Mazzucchelli G, Picariello G, Romero-Sahagun A, Villa C, Roncada P, Molina E. New applications of advanced instrumental techniques for the characterization of food allergenic proteins. in Critical Reviews in Food Science and Nutrition. 2022;62(31).
doi:10.1080/10408398.2021.1931806 .
Benedé, Sara, Lozano-Ojalvo, Daniel, Cristobal, Susana, Costa, Joana, D’Auria, Enza, Ćirković-Veličković, Tanja, Garrido-Arandia, María, Karakaya, Sibel, Mafra, Isabel, Mazzucchelli, Gabriel, Picariello, Gianluca, Romero-Sahagun, Alejandro, Villa, Caterina, Roncada, Paola, Molina, Elena, "New applications of advanced instrumental techniques for the characterization of food allergenic proteins" in Critical Reviews in Food Science and Nutrition, 62, no. 31 (2022),
https://doi.org/10.1080/10408398.2021.1931806 . .
1
7
2
8

Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?

Costa, Joana; Bavaro, Simona Lucia; Benedé, Sara; Diaz-Perales, Araceli; Bueno-Diaz, Cristina; Gelencser, Eva; Klueber, Julia; Larré, Colette; Lozano-Ojalvo, Daniel; Lupi, Roberta; Mafra, Isabel; Mazzucchelli, Gabriel; Molina, Elena; Monaci, Linda; Martín-Pedraza, Laura; Piras, Cristian; Rodrigues, Pedro M.; Roncada, Paola; Schrama, Denise; Ćirković-Veličković, Tanja; Verhoeckx, Kitty; Villa, Caterina; Kuehn, Annette; Hoffmann-Sommergruber, Karin; Holzhauser, Thomas

(Springer, 2022)

TY  - JOUR
AU  - Costa, Joana
AU  - Bavaro, Simona Lucia
AU  - Benedé, Sara
AU  - Diaz-Perales, Araceli
AU  - Bueno-Diaz, Cristina
AU  - Gelencser, Eva
AU  - Klueber, Julia
AU  - Larré, Colette
AU  - Lozano-Ojalvo, Daniel
AU  - Lupi, Roberta
AU  - Mafra, Isabel
AU  - Mazzucchelli, Gabriel
AU  - Molina, Elena
AU  - Monaci, Linda
AU  - Martín-Pedraza, Laura
AU  - Piras, Cristian
AU  - Rodrigues, Pedro M.
AU  - Roncada, Paola
AU  - Schrama, Denise
AU  - Ćirković-Veličković, Tanja
AU  - Verhoeckx, Kitty
AU  - Villa, Caterina
AU  - Kuehn, Annette
AU  - Hoffmann-Sommergruber, Karin
AU  - Holzhauser, Thomas
PY  - 2022
UR  - https://doi.org/10.1007/s12016-020-08810-9
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4981
AB  - This review searched for published evidence that could explain how different physicochemical properties impact on the allergenicity of food proteins and if their effects would follow specific patterns among distinct protein families. Owing to the amount and complexity of the collected information, this literature overview was divided in two articles, the current one dedicated to protein families of plant allergens and a second one focused on animal allergens. Our extensive analysis of the available literature revealed that physicochemical characteristics had consistent effects on protein allergenicity for allergens belonging to the same protein family. For example, protein aggregation contributes to increased allergenicity of 2S albumins, while for legumins and cereal prolamins, the same phenomenon leads to a reduction. Molecular stability, related to structural resistance to heat and proteolysis, was identified as the most common feature promoting plant protein allergenicity, although it fails to explain the potency of some unstable allergens (e.g. pollen-related food allergens). Furthermore, data on physicochemical characteristics translating into clinical effects are limited, mainly because most studies are focused on in vitro IgE binding. Clinical data assessing how these parameters affect the development and clinical manifestation of allergies is minimal, with only few reports evaluating the sensitising capacity of modified proteins (addressing different physicochemical properties) in murine allergy models. In vivo testing of modified pure proteins by SPT or DBPCFC is scarce. At this stage, a systematic approach to link the physicochemical properties with clinical plant allergenicity in real-life scenarios is still missing.
PB  - Springer
T2  - Clinical Reviews in Allergy & Immunology
T1  - Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?
VL  - 62
IS  - 1
SP  - 37
EP  - 63
DO  - 10.1007/s12016-020-08810-9
ER  - 
@article{
author = "Costa, Joana and Bavaro, Simona Lucia and Benedé, Sara and Diaz-Perales, Araceli and Bueno-Diaz, Cristina and Gelencser, Eva and Klueber, Julia and Larré, Colette and Lozano-Ojalvo, Daniel and Lupi, Roberta and Mafra, Isabel and Mazzucchelli, Gabriel and Molina, Elena and Monaci, Linda and Martín-Pedraza, Laura and Piras, Cristian and Rodrigues, Pedro M. and Roncada, Paola and Schrama, Denise and Ćirković-Veličković, Tanja and Verhoeckx, Kitty and Villa, Caterina and Kuehn, Annette and Hoffmann-Sommergruber, Karin and Holzhauser, Thomas",
year = "2022",
abstract = "This review searched for published evidence that could explain how different physicochemical properties impact on the allergenicity of food proteins and if their effects would follow specific patterns among distinct protein families. Owing to the amount and complexity of the collected information, this literature overview was divided in two articles, the current one dedicated to protein families of plant allergens and a second one focused on animal allergens. Our extensive analysis of the available literature revealed that physicochemical characteristics had consistent effects on protein allergenicity for allergens belonging to the same protein family. For example, protein aggregation contributes to increased allergenicity of 2S albumins, while for legumins and cereal prolamins, the same phenomenon leads to a reduction. Molecular stability, related to structural resistance to heat and proteolysis, was identified as the most common feature promoting plant protein allergenicity, although it fails to explain the potency of some unstable allergens (e.g. pollen-related food allergens). Furthermore, data on physicochemical characteristics translating into clinical effects are limited, mainly because most studies are focused on in vitro IgE binding. Clinical data assessing how these parameters affect the development and clinical manifestation of allergies is minimal, with only few reports evaluating the sensitising capacity of modified proteins (addressing different physicochemical properties) in murine allergy models. In vivo testing of modified pure proteins by SPT or DBPCFC is scarce. At this stage, a systematic approach to link the physicochemical properties with clinical plant allergenicity in real-life scenarios is still missing.",
publisher = "Springer",
journal = "Clinical Reviews in Allergy & Immunology",
title = "Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?",
volume = "62",
number = "1",
pages = "37-63",
doi = "10.1007/s12016-020-08810-9"
}
Costa, J., Bavaro, S. L., Benedé, S., Diaz-Perales, A., Bueno-Diaz, C., Gelencser, E., Klueber, J., Larré, C., Lozano-Ojalvo, D., Lupi, R., Mafra, I., Mazzucchelli, G., Molina, E., Monaci, L., Martín-Pedraza, L., Piras, C., Rodrigues, P. M., Roncada, P., Schrama, D., Ćirković-Veličković, T., Verhoeckx, K., Villa, C., Kuehn, A., Hoffmann-Sommergruber, K.,& Holzhauser, T.. (2022). Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?. in Clinical Reviews in Allergy & Immunology
Springer., 62(1), 37-63.
https://doi.org/10.1007/s12016-020-08810-9
Costa J, Bavaro SL, Benedé S, Diaz-Perales A, Bueno-Diaz C, Gelencser E, Klueber J, Larré C, Lozano-Ojalvo D, Lupi R, Mafra I, Mazzucchelli G, Molina E, Monaci L, Martín-Pedraza L, Piras C, Rodrigues PM, Roncada P, Schrama D, Ćirković-Veličković T, Verhoeckx K, Villa C, Kuehn A, Hoffmann-Sommergruber K, Holzhauser T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?. in Clinical Reviews in Allergy & Immunology. 2022;62(1):37-63.
doi:10.1007/s12016-020-08810-9 .
Costa, Joana, Bavaro, Simona Lucia, Benedé, Sara, Diaz-Perales, Araceli, Bueno-Diaz, Cristina, Gelencser, Eva, Klueber, Julia, Larré, Colette, Lozano-Ojalvo, Daniel, Lupi, Roberta, Mafra, Isabel, Mazzucchelli, Gabriel, Molina, Elena, Monaci, Linda, Martín-Pedraza, Laura, Piras, Cristian, Rodrigues, Pedro M., Roncada, Paola, Schrama, Denise, Ćirković-Veličković, Tanja, Verhoeckx, Kitty, Villa, Caterina, Kuehn, Annette, Hoffmann-Sommergruber, Karin, Holzhauser, Thomas, "Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens?" in Clinical Reviews in Allergy & Immunology, 62, no. 1 (2022):37-63,
https://doi.org/10.1007/s12016-020-08810-9 . .
9
62
30
55

Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.

Costa, Joana; Bavaro, Simona Lucia; Benedé, Sara; Diaz-Perales, Araceli; Bueno-Diaz, Cristina; Gelencser, Eva; Klueber, Julia; Larré, Colette; Lozano-Ojalvo, Daniel; Lupi, Roberta; Mafra, Isabel; Mazzucchelli, Gabriel; Molina, Elena; Monaci, Linda; Martín-Pedraza, Laura; Piras, Cristian; Rodrigues, Pedro M.; Roncada, Paola; Schrama, Denise; Ćirković-Veličković, Tanja; Verhoeckx, Kitty; Villa, Caterina; Kuehn, Annette; Hoffmann-Sommergruber, Karin; Holzhauser, Thomas

(Springer, 2022)

TY  - DATA
AU  - Costa, Joana
AU  - Bavaro, Simona Lucia
AU  - Benedé, Sara
AU  - Diaz-Perales, Araceli
AU  - Bueno-Diaz, Cristina
AU  - Gelencser, Eva
AU  - Klueber, Julia
AU  - Larré, Colette
AU  - Lozano-Ojalvo, Daniel
AU  - Lupi, Roberta
AU  - Mafra, Isabel
AU  - Mazzucchelli, Gabriel
AU  - Molina, Elena
AU  - Monaci, Linda
AU  - Martín-Pedraza, Laura
AU  - Piras, Cristian
AU  - Rodrigues, Pedro M.
AU  - Roncada, Paola
AU  - Schrama, Denise
AU  - Ćirković-Veličković, Tanja
AU  - Verhoeckx, Kitty
AU  - Villa, Caterina
AU  - Kuehn, Annette
AU  - Hoffmann-Sommergruber, Karin
AU  - Holzhauser, Thomas
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4982
PB  - Springer
T2  - Clinical Reviews in Allergy & Immunology
T1  - Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4982
ER  - 
@misc{
author = "Costa, Joana and Bavaro, Simona Lucia and Benedé, Sara and Diaz-Perales, Araceli and Bueno-Diaz, Cristina and Gelencser, Eva and Klueber, Julia and Larré, Colette and Lozano-Ojalvo, Daniel and Lupi, Roberta and Mafra, Isabel and Mazzucchelli, Gabriel and Molina, Elena and Monaci, Linda and Martín-Pedraza, Laura and Piras, Cristian and Rodrigues, Pedro M. and Roncada, Paola and Schrama, Denise and Ćirković-Veličković, Tanja and Verhoeckx, Kitty and Villa, Caterina and Kuehn, Annette and Hoffmann-Sommergruber, Karin and Holzhauser, Thomas",
year = "2022",
publisher = "Springer",
journal = "Clinical Reviews in Allergy & Immunology",
title = "Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4982"
}
Costa, J., Bavaro, S. L., Benedé, S., Diaz-Perales, A., Bueno-Diaz, C., Gelencser, E., Klueber, J., Larré, C., Lozano-Ojalvo, D., Lupi, R., Mafra, I., Mazzucchelli, G., Molina, E., Monaci, L., Martín-Pedraza, L., Piras, C., Rodrigues, P. M., Roncada, P., Schrama, D., Ćirković-Veličković, T., Verhoeckx, K., Villa, C., Kuehn, A., Hoffmann-Sommergruber, K.,& Holzhauser, T.. (2022). Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.. in Clinical Reviews in Allergy & Immunology
Springer..
https://hdl.handle.net/21.15107/rcub_cherry_4982
Costa J, Bavaro SL, Benedé S, Diaz-Perales A, Bueno-Diaz C, Gelencser E, Klueber J, Larré C, Lozano-Ojalvo D, Lupi R, Mafra I, Mazzucchelli G, Molina E, Monaci L, Martín-Pedraza L, Piras C, Rodrigues PM, Roncada P, Schrama D, Ćirković-Veličković T, Verhoeckx K, Villa C, Kuehn A, Hoffmann-Sommergruber K, Holzhauser T. Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9.. in Clinical Reviews in Allergy & Immunology. 2022;.
https://hdl.handle.net/21.15107/rcub_cherry_4982 .
Costa, Joana, Bavaro, Simona Lucia, Benedé, Sara, Diaz-Perales, Araceli, Bueno-Diaz, Cristina, Gelencser, Eva, Klueber, Julia, Larré, Colette, Lozano-Ojalvo, Daniel, Lupi, Roberta, Mafra, Isabel, Mazzucchelli, Gabriel, Molina, Elena, Monaci, Linda, Martín-Pedraza, Laura, Piras, Cristian, Rodrigues, Pedro M., Roncada, Paola, Schrama, Denise, Ćirković-Veličković, Tanja, Verhoeckx, Kitty, Villa, Caterina, Kuehn, Annette, Hoffmann-Sommergruber, Karin, Holzhauser, Thomas, "Supplementary data for the article: Costa, J.; Bavaro, S. L.; Benedé, S.; Diaz-Perales, A.; Bueno-Diaz, C.; Gelencser, E.; Klueber, J.; Larré, C.; Lozano-Ojalvo, D.; Lupi, R.; Mafra, I.; Mazzucchelli, G.; Molina, E.; Monaci, L.; Martín-Pedraza, L.; Piras, C.; Rodrigues, P. M.; Roncada, P.; Schrama, D.; Cirkovic-Velickovic, T.; Verhoeckx, K.; Villa, C.; Kuehn, A.; Hoffmann-Sommergruber, K.; Holzhauser, T. Are Physicochemical Properties Shaping the Allergenic Potency of Plant Allergens? Clinic Rev Allerg Immunol 2022, 62 (1), 37–63. https://doi.org/10.1007/s12016-020-08810-9." in Clinical Reviews in Allergy & Immunology (2022),
https://hdl.handle.net/21.15107/rcub_cherry_4982 .