FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics

Link to this page

info:eu-repo/grantAgreement/EC/H2020/810752/EU//

FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics (en)
Authors

Publications

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 . .

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 . .

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

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

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 .

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 .

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 .

Electronic cigarette liquids impair protein synthesis and alter proteomic profiles in V79 cells

Ljujic, Mila; Trifunović, Sara; Smiljanić, Katarina; Solari, Fiorella Andrea; Sickmann, Albert; Divac Rankov, Aleksandra

(European Respiraotory Society (ERS), 2022)

TY  - CONF
AU  - Ljujic, Mila
AU  - Trifunović, Sara
AU  - Smiljanić, Katarina
AU  - Solari, Fiorella Andrea
AU  - Sickmann, Albert
AU  - Divac Rankov, Aleksandra
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5731
AB  - The COVID-19 pandemic caused by the SARS-CoV2 virus poses a global health threat with over 5 million deaths recorded. There is little understanding regarding SARS-CoV2 pathogenesis in the human airways and disease severity increases with age. Neutrophils are white blood cells found in large numbers in the airways of the lungs in severe COVID-19 patients. It is not known whether this influx of neutrophils into the airway has a protective or detrimental effect. We aim to understand the role of neutrophils during COVID-19 pathology, using an experimental infection model of the airway epithelium from the eldelry and children. To do this, we collect nasal airway cells from healthy elderly and children and grow them at air-liquid interface. Once differentiation and ciliation of these cells is reached, we infect the cells with SARS-CoV2 virus and allow neutrophils to migrate from the basolateral (blood) to the apical (air) side of the epithelium, similar to a physiological airway. Using flow cytometric analyses, we measure the expression of activation markers and the number of neutrophils that migrate across the epithelium of different ages in response to SARS-CoV2 infection. Preliminary work shows less viable neutrophils recovered from the elderly epithelium, more activated neutrophils when migrating through the elderly epithelium, as well as increased numbers of neutrophils remaining on the basolateral (blood) side of the elderly epithelium. These findings point to an inflammatory neutrophil phenotype influenced by the damaged elderly epithelium and supports the hypothesis that neutrophils are responsible for the severity of disease.
PB  - European Respiraotory Society (ERS)
C3  - European Respiratory Journal
T1  - Electronic cigarette liquids impair protein synthesis and alter proteomic profiles in V79 cells
VL  - 60
IS  - 66
SP  - 506
DO  - 10.1183/13993003.congress-2022.506
ER  - 
@conference{
author = "Ljujic, Mila and Trifunović, Sara and Smiljanić, Katarina and Solari, Fiorella Andrea and Sickmann, Albert and Divac Rankov, Aleksandra",
year = "2022",
abstract = "The COVID-19 pandemic caused by the SARS-CoV2 virus poses a global health threat with over 5 million deaths recorded. There is little understanding regarding SARS-CoV2 pathogenesis in the human airways and disease severity increases with age. Neutrophils are white blood cells found in large numbers in the airways of the lungs in severe COVID-19 patients. It is not known whether this influx of neutrophils into the airway has a protective or detrimental effect. We aim to understand the role of neutrophils during COVID-19 pathology, using an experimental infection model of the airway epithelium from the eldelry and children. To do this, we collect nasal airway cells from healthy elderly and children and grow them at air-liquid interface. Once differentiation and ciliation of these cells is reached, we infect the cells with SARS-CoV2 virus and allow neutrophils to migrate from the basolateral (blood) to the apical (air) side of the epithelium, similar to a physiological airway. Using flow cytometric analyses, we measure the expression of activation markers and the number of neutrophils that migrate across the epithelium of different ages in response to SARS-CoV2 infection. Preliminary work shows less viable neutrophils recovered from the elderly epithelium, more activated neutrophils when migrating through the elderly epithelium, as well as increased numbers of neutrophils remaining on the basolateral (blood) side of the elderly epithelium. These findings point to an inflammatory neutrophil phenotype influenced by the damaged elderly epithelium and supports the hypothesis that neutrophils are responsible for the severity of disease.",
publisher = "European Respiraotory Society (ERS)",
journal = "European Respiratory Journal",
title = "Electronic cigarette liquids impair protein synthesis and alter proteomic profiles in V79 cells",
volume = "60",
number = "66",
pages = "506",
doi = "10.1183/13993003.congress-2022.506"
}
Ljujic, M., Trifunović, S., Smiljanić, K., Solari, F. A., Sickmann, A.,& Divac Rankov, A.. (2022). Electronic cigarette liquids impair protein synthesis and alter proteomic profiles in V79 cells. in European Respiratory Journal
European Respiraotory Society (ERS)., 60(66), 506.
https://doi.org/10.1183/13993003.congress-2022.506
Ljujic M, Trifunović S, Smiljanić K, Solari FA, Sickmann A, Divac Rankov A. Electronic cigarette liquids impair protein synthesis and alter proteomic profiles in V79 cells. in European Respiratory Journal. 2022;60(66):506.
doi:10.1183/13993003.congress-2022.506 .
Ljujic, Mila, Trifunović, Sara, Smiljanić, Katarina, Solari, Fiorella Andrea, Sickmann, Albert, Divac Rankov, Aleksandra, "Electronic cigarette liquids impair protein synthesis and alter proteomic profiles in V79 cells" in European Respiratory Journal, 60, no. 66 (2022):506,
https://doi.org/10.1183/13993003.congress-2022.506 . .

Ispitivanje regioselektivnosti Zr-Wells-Dawson 1:2 polioksometalata na β-laktoglobulinu kao model proteinu

Bajkanović, Dragana

(2022)

TY  - THES
AU  - Bajkanović, Dragana
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5469
AB  - Cilj ovog rada je bio ispitati regioselektivnost Zr-Wells-Dawson 1:2 polioksometalata (Zr-WD 1:2) na β-laktoglobulinu (BLG) kao model proteinu. Literaturni podaci ukazuju na selektivnost ka kiselim aminokiselinama, kao što su aspartat i glutamat. Kako bismo dobili što pouzdanije rezultate u radu su korišteni nativni BLG (smjesa A i B izoforme), redukovan i alkilovan BLG i pojedinačne izoforme A i B. Rezultati dobijeni reakcijom sa Zr-WD 1:2 ukazuju da dolazi do hidrolize i da je elektroforetski profil različit za sve ispitivane tipove BLG. Zbog uslova reakcije (7 dana na 60 °C) dolazi i do autolize tako da krajnji efekat jeste kombinovani efekat autolize i dejstva Zr-WD 1:2. Bitno za naglasiti jeste to da nakon 24 časa na elektroforetskim profilma se javljaju proizvodi hidrolize, dok autoliza izostaje. Takođe, rezultati su pokazali da Zr-WD 1:2 ne ispoljava isključivu selektivnost ka kiselim aminokiselinama (aspartatu i glutamatu) već dolazi do hidrolize i na drugim aminokiselinama što nije u skladu sa literaturnim podacima u uzorku redukovanog i alkilovanog BLG.
T1  - Ispitivanje regioselektivnosti Zr-Wells-Dawson 1:2 polioksometalata na β-laktoglobulinu kao model proteinu
SP  - 1
EP  - 67
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5469
ER  - 
@mastersthesis{
author = "Bajkanović, Dragana",
year = "2022",
abstract = "Cilj ovog rada je bio ispitati regioselektivnost Zr-Wells-Dawson 1:2 polioksometalata (Zr-WD 1:2) na β-laktoglobulinu (BLG) kao model proteinu. Literaturni podaci ukazuju na selektivnost ka kiselim aminokiselinama, kao što su aspartat i glutamat. Kako bismo dobili što pouzdanije rezultate u radu su korišteni nativni BLG (smjesa A i B izoforme), redukovan i alkilovan BLG i pojedinačne izoforme A i B. Rezultati dobijeni reakcijom sa Zr-WD 1:2 ukazuju da dolazi do hidrolize i da je elektroforetski profil različit za sve ispitivane tipove BLG. Zbog uslova reakcije (7 dana na 60 °C) dolazi i do autolize tako da krajnji efekat jeste kombinovani efekat autolize i dejstva Zr-WD 1:2. Bitno za naglasiti jeste to da nakon 24 časa na elektroforetskim profilma se javljaju proizvodi hidrolize, dok autoliza izostaje. Takođe, rezultati su pokazali da Zr-WD 1:2 ne ispoljava isključivu selektivnost ka kiselim aminokiselinama (aspartatu i glutamatu) već dolazi do hidrolize i na drugim aminokiselinama što nije u skladu sa literaturnim podacima u uzorku redukovanog i alkilovanog BLG.",
title = "Ispitivanje regioselektivnosti Zr-Wells-Dawson 1:2 polioksometalata na β-laktoglobulinu kao model proteinu",
pages = "1-67",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5469"
}
Bajkanović, D.. (2022). Ispitivanje regioselektivnosti Zr-Wells-Dawson 1:2 polioksometalata na β-laktoglobulinu kao model proteinu. , 1-67.
https://hdl.handle.net/21.15107/rcub_cherry_5469
Bajkanović D. Ispitivanje regioselektivnosti Zr-Wells-Dawson 1:2 polioksometalata na β-laktoglobulinu kao model proteinu. 2022;:1-67.
https://hdl.handle.net/21.15107/rcub_cherry_5469 .
Bajkanović, Dragana, "Ispitivanje regioselektivnosti Zr-Wells-Dawson 1:2 polioksometalata na β-laktoglobulinu kao model proteinu" (2022):1-67,
https://hdl.handle.net/21.15107/rcub_cherry_5469 .

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

Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells

Trifunović, Sara; Smiljanić, Katarina; Sickmann, Albert; Solari, Fiorella Andrea; Kolarević, Stoimir; Divac Rankov, Aleksandra; Ljujic, Mila

(BMC Springer Nature, 2022)

TY  - JOUR
AU  - Trifunović, Sara
AU  - Smiljanić, Katarina
AU  - Sickmann, Albert
AU  - Solari, Fiorella Andrea
AU  - Kolarević, Stoimir
AU  - Divac Rankov, Aleksandra
AU  - Ljujic, Mila
PY  - 2022
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5458
AB  - Abstract
Background: Although still considered a safer alternative to classical cigarettes, growing body of work points to
harmful effects of electronic cigarettes (e-cigarettes) affecting a range of cellular processes. The biological effect of
e-cigarettes needs to be investigated in more detail considering their widespread use.
Methods: In this study, we treated V79 lung fibroblasts with sub-cytotoxic concentration of e-cigarette liquids, with
and without nicotine. Mutagenicity was evaluated by HPRT assay, genotoxicity by comet assay and the effect on cel-
lular communication by metabolic cooperation assay. Additionally, comprehensive proteome analysis was performed
via high resolution, parallel accumulation serial fragmentation-PASEF mass spectrometry.
Results: E-cigarette liquid concentration used in this study showed no mutagenic or genotoxic effect, however it
negatively impacted metabolic cooperation between V79 cells. Both e-cigarette liquids induced significant depletion
in total number of proteins and impairment of mitochondrial function in treated cells. The focal adhesion proteins
were upregulated, which is in accordance with the results of metabolic cooperation assay. Increased presence of post-
translational modifications (PTMs), including carbonylation and direct oxidative modifications, was observed. Data are
available via ProteomeXchange with identifier PXD032071.
Conclusions: Our study revealed impairment of metabolic cooperation as well as significant proteome and PTMs
alterations in V79 cells treated with e-cigarette liquid warranting future studies on e-cigarettes health impact.
PB  - BMC Springer Nature
T2  - Respiratory Research
T1  - Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells
VL  - 23
IS  - 191
DO  - 10.1186/s12931-022-02102-w
ER  - 
@article{
author = "Trifunović, Sara and Smiljanić, Katarina and Sickmann, Albert and Solari, Fiorella Andrea and Kolarević, Stoimir and Divac Rankov, Aleksandra and Ljujic, Mila",
year = "2022",
abstract = "Abstract
Background: Although still considered a safer alternative to classical cigarettes, growing body of work points to
harmful effects of electronic cigarettes (e-cigarettes) affecting a range of cellular processes. The biological effect of
e-cigarettes needs to be investigated in more detail considering their widespread use.
Methods: In this study, we treated V79 lung fibroblasts with sub-cytotoxic concentration of e-cigarette liquids, with
and without nicotine. Mutagenicity was evaluated by HPRT assay, genotoxicity by comet assay and the effect on cel-
lular communication by metabolic cooperation assay. Additionally, comprehensive proteome analysis was performed
via high resolution, parallel accumulation serial fragmentation-PASEF mass spectrometry.
Results: E-cigarette liquid concentration used in this study showed no mutagenic or genotoxic effect, however it
negatively impacted metabolic cooperation between V79 cells. Both e-cigarette liquids induced significant depletion
in total number of proteins and impairment of mitochondrial function in treated cells. The focal adhesion proteins
were upregulated, which is in accordance with the results of metabolic cooperation assay. Increased presence of post-
translational modifications (PTMs), including carbonylation and direct oxidative modifications, was observed. Data are
available via ProteomeXchange with identifier PXD032071.
Conclusions: Our study revealed impairment of metabolic cooperation as well as significant proteome and PTMs
alterations in V79 cells treated with e-cigarette liquid warranting future studies on e-cigarettes health impact.",
publisher = "BMC Springer Nature",
journal = "Respiratory Research",
title = "Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells",
volume = "23",
number = "191",
doi = "10.1186/s12931-022-02102-w"
}
Trifunović, S., Smiljanić, K., Sickmann, A., Solari, F. A., Kolarević, S., Divac Rankov, A.,& Ljujic, M.. (2022). Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells. in Respiratory Research
BMC Springer Nature., 23(191).
https://doi.org/10.1186/s12931-022-02102-w
Trifunović S, Smiljanić K, Sickmann A, Solari FA, Kolarević S, Divac Rankov A, Ljujic M. Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells. in Respiratory Research. 2022;23(191).
doi:10.1186/s12931-022-02102-w .
Trifunović, Sara, Smiljanić, Katarina, Sickmann, Albert, Solari, Fiorella Andrea, Kolarević, Stoimir, Divac Rankov, Aleksandra, Ljujic, Mila, "Electronic cigarette liquids impair metabolic cooperation and alter proteomic profiles in V79 cells" in Respiratory Research, 23, no. 191 (2022),
https://doi.org/10.1186/s12931-022-02102-w . .
9

Trypsin as a proteomic probe to assess food protein digestibility in relation to post- translational modifications

Smiljanić, Katarina; Prodić, Ivana; Đukić, Teodora; Vasović, Tamara; Jovanović, Vesna; Ćirković-Veličković, Tanja

(INFOGEST Cost action, INRAE, Teagasc LTD., 2021)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Prodić, Ivana
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Jovanović, Vesna
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5773
AB  - Background: We have undertaken study on our porcine-derived trypsin generated
proteomic data of the major peanut allergen Ara h 1 from the raw and roasted peanut, to
assess possible facilitating/hindrance effects on trypsin digestion efficacy caused by post-
translational and chemical modifications (PTMs) positioned on K/R residues. If potential
hindrance effects caused by PTMs are observed with porcine trypsin, then they can be just
augmented and more pronounced within human intestinal digestion. The logic for such
reasoning is in inferior performance of human trypsin compared to porcine-derived used in
proteomic digestion protocols, also the lower trypsin-to-sample ratio and much shorter
digestion times, even though gastric digestion precedes and trypsin is not the sole digestive
enzyme.
Methods: Novel method was developed to decipher outcomes at scissile bonds using PEAKS
Studio-X+ in reassessment of high-resolution tandem mass spectrometry data on 18h-long
trypsin digestion protocol.
Results: In eight modified K/R residues involving methylation, dihydroxy and formylation,
differences in extent of miscleavage between modified and unmodified peptides, were
significantly higher (>10%) in modified peptides.
Conclusion: It is important to elucidate impact of modifications on trypsin digestion
performance, but also on other proteases involved in digestion process due to possible
effects on allergenicity of food proteins/peptides.
PB  - INFOGEST Cost action, INRAE, Teagasc LTD.
C3  - Virtual International Conference on Food Digestion 6th and 7th May, 2021
T1  - Trypsin as a proteomic probe to assess food protein digestibility in relation to post- translational modifications
SP  - 18
EP  - 18
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5773
ER  - 
@conference{
author = "Smiljanić, Katarina and Prodić, Ivana and Đukić, Teodora and Vasović, Tamara and Jovanović, Vesna and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Background: We have undertaken study on our porcine-derived trypsin generated
proteomic data of the major peanut allergen Ara h 1 from the raw and roasted peanut, to
assess possible facilitating/hindrance effects on trypsin digestion efficacy caused by post-
translational and chemical modifications (PTMs) positioned on K/R residues. If potential
hindrance effects caused by PTMs are observed with porcine trypsin, then they can be just
augmented and more pronounced within human intestinal digestion. The logic for such
reasoning is in inferior performance of human trypsin compared to porcine-derived used in
proteomic digestion protocols, also the lower trypsin-to-sample ratio and much shorter
digestion times, even though gastric digestion precedes and trypsin is not the sole digestive
enzyme.
Methods: Novel method was developed to decipher outcomes at scissile bonds using PEAKS
Studio-X+ in reassessment of high-resolution tandem mass spectrometry data on 18h-long
trypsin digestion protocol.
Results: In eight modified K/R residues involving methylation, dihydroxy and formylation,
differences in extent of miscleavage between modified and unmodified peptides, were
significantly higher (>10%) in modified peptides.
Conclusion: It is important to elucidate impact of modifications on trypsin digestion
performance, but also on other proteases involved in digestion process due to possible
effects on allergenicity of food proteins/peptides.",
publisher = "INFOGEST Cost action, INRAE, Teagasc LTD.",
journal = "Virtual International Conference on Food Digestion 6th and 7th May, 2021",
title = "Trypsin as a proteomic probe to assess food protein digestibility in relation to post- translational modifications",
pages = "18-18",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5773"
}
Smiljanić, K., Prodić, I., Đukić, T., Vasović, T., Jovanović, V.,& Ćirković-Veličković, T.. (2021). Trypsin as a proteomic probe to assess food protein digestibility in relation to post- translational modifications. in Virtual International Conference on Food Digestion 6th and 7th May, 2021
INFOGEST Cost action, INRAE, Teagasc LTD.., 18-18.
https://hdl.handle.net/21.15107/rcub_cherry_5773
Smiljanić K, Prodić I, Đukić T, Vasović T, Jovanović V, Ćirković-Veličković T. Trypsin as a proteomic probe to assess food protein digestibility in relation to post- translational modifications. in Virtual International Conference on Food Digestion 6th and 7th May, 2021. 2021;:18-18.
https://hdl.handle.net/21.15107/rcub_cherry_5773 .
Smiljanić, Katarina, Prodić, Ivana, Đukić, Teodora, Vasović, Tamara, Jovanović, Vesna, Ćirković-Veličković, Tanja, "Trypsin as a proteomic probe to assess food protein digestibility in relation to post- translational modifications" in Virtual International Conference on Food Digestion 6th and 7th May, 2021 (2021):18-18,
https://hdl.handle.net/21.15107/rcub_cherry_5773 .

Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart

Prodić, Ivana; Smiljanić, Katarina; Hoffmann-Sommergruber, Karin; Ćirković-Veličković, Tanja

(INFOGEST Cost action, INRAE, Teagasc LTD., 2021)

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5772
AB  - Background: In vitro pepsin digestion is important factor when assessing protein food
allergenicity. Roasted hazelnut is more common in human nutrition than a raw hazelnut;
however, all studies were focused on Cor a 9 allergen obtained from a raw hazelnut. There
are only two studies employing in vitro INFOGEST digestion harmonized protocol on
hazelnut with its full matrix. The aim of this study was to assess immunoreactivity of raw
and roasted hazelnut gastric digests and to compare secondary/tertiary structure of Cor a 9
allergen purified from these two sources.
Methods: Digestion resistant protein fragments were analysed by 1D/2D electrophoresis.
Following digestion, IgE binding from patients’ pooled sera and by specific antibodies, were
assessed in ELISA and immunoblot. CD spectroscopy was applied for Cor a 9 structural
analyses.
Results: Cor a 11 and acidic forms of Cor a 9 were more prone to pepsin proteolysis, yet
their large fragments survived partially. Cor a 8 was protected by lipids, retaining capability
to bind its specific antibody. Roasting did not significantly affect secondary structure of the
most abundant hazelnut allergen, Cor a 9.
Conclusion: Roasting of hazelnut seems to boost IgE binding derived from pooled sera of
hazelnut allergic patients with oral-gastric allergen digests.
PB  - INFOGEST Cost action, INRAE, Teagasc LTD.
C3  - Virtual International Conference on Food Digestion 6th and 7th May, 2021
T1  - Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart
SP  - 62
EP  - 62
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5772
ER  - 
@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Background: In vitro pepsin digestion is important factor when assessing protein food
allergenicity. Roasted hazelnut is more common in human nutrition than a raw hazelnut;
however, all studies were focused on Cor a 9 allergen obtained from a raw hazelnut. There
are only two studies employing in vitro INFOGEST digestion harmonized protocol on
hazelnut with its full matrix. The aim of this study was to assess immunoreactivity of raw
and roasted hazelnut gastric digests and to compare secondary/tertiary structure of Cor a 9
allergen purified from these two sources.
Methods: Digestion resistant protein fragments were analysed by 1D/2D electrophoresis.
Following digestion, IgE binding from patients’ pooled sera and by specific antibodies, were
assessed in ELISA and immunoblot. CD spectroscopy was applied for Cor a 9 structural
analyses.
Results: Cor a 11 and acidic forms of Cor a 9 were more prone to pepsin proteolysis, yet
their large fragments survived partially. Cor a 8 was protected by lipids, retaining capability
to bind its specific antibody. Roasting did not significantly affect secondary structure of the
most abundant hazelnut allergen, Cor a 9.
Conclusion: Roasting of hazelnut seems to boost IgE binding derived from pooled sera of
hazelnut allergic patients with oral-gastric allergen digests.",
publisher = "INFOGEST Cost action, INRAE, Teagasc LTD.",
journal = "Virtual International Conference on Food Digestion 6th and 7th May, 2021",
title = "Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart",
pages = "62-62",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5772"
}
Prodić, I., Smiljanić, K., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2021). Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart. in Virtual International Conference on Food Digestion 6th and 7th May, 2021
INFOGEST Cost action, INRAE, Teagasc LTD.., 62-62.
https://hdl.handle.net/21.15107/rcub_cherry_5772
Prodić I, Smiljanić K, Hoffmann-Sommergruber K, Ćirković-Veličković T. Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart. in Virtual International Conference on Food Digestion 6th and 7th May, 2021. 2021;:62-62.
https://hdl.handle.net/21.15107/rcub_cherry_5772 .
Prodić, Ivana, Smiljanić, Katarina, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Allergome of oral-gastric in vitro digest of roasted hazelnut shows stronger IgE binding compared to the raw counterpart" in Virtual International Conference on Food Digestion 6th and 7th May, 2021 (2021):62-62,
https://hdl.handle.net/21.15107/rcub_cherry_5772 .

Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol

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

(Sociedade Portuguesa de Química, 2021)

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Nagl, Christoph
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5762
AB  - Cor a 8 is a relevant allergen that can cause severe allergic reactions. It is a 115 amino acid protein with a molecular mass of 9 kDa and is a member of the non-specific lipida transfer protein family. This allergen is resistant to high temperatures, pH changes, gastric and intestinal enzymes. The main route of exposure is through ingestion. In order to examine its resistance to digestion, we have applied a popular 1.0 INFOGEST protocol [1], specialized for the complete food, which in vitro mimics physiologically relevant conditions of oral-gastric-intestinal digestion. The aim of this study was to compare Cor a 8 resistance to gastric digestion, from both, raw and roasted hazelnuts, before and upon pepsin (gastric) digestion. Stability of the Cor a 8 protein was investigated by simulation of oral and gastric digestion phases, performed with ground raw and roasted hazelnut kernels. Hazelnut proteins were extracted from the digestion mixture and analyzed by 1D and 2D SDS-PAGE, while raw and roasted Cor a 8 western blots were probed with specific anti-Cor a 8 antibodies in 1D and 2D immunoblots. The electrophoretic patterns of the raw and roasted extracts were similar. 1D SDS PAGE profiles demonstrated high stability of Cor a 8 against enzymatic treatments. Control samples of Cor a 8 from raw and roasted hazelnut extracts migrated as a single band at around 12 kDa in 1D immunoblot. However, in case of roasted hazelnut, the protein showed a slightly lower capacity to bind specific anti-Cor a 8 antibody, as compared to raw hazelnut extract. In 2D immunoblot, with higher resolution, specific antibody binding was decting a significant and noticeable smear in the basic region indicating a range of different protein variants. This was more pronounced detectable in the case of roasted sample upon digestion, pointing to a mix of variants in this allergen batch. It has been suggested that the allergenicity of the Cor a 8 is almost insensitive to temperature. The allergen is stable even after digestion and roasting processes up to 140˚C. We hypothesize that a lipid-rich food matrix delays extraction of proteins, thereby delaying their gastrointestinal digestion, which may affect allergen sensitizing capacity and clinical symptoms.
PB  - Sociedade Portuguesa de Química
C3  - Book of Abstracts of the XXI EuroFoodChem Congress
T1  - Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol
SP  - 126
EP  - 126
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5762
ER  - 
@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Nagl, Christoph and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Cor a 8 is a relevant allergen that can cause severe allergic reactions. It is a 115 amino acid protein with a molecular mass of 9 kDa and is a member of the non-specific lipida transfer protein family. This allergen is resistant to high temperatures, pH changes, gastric and intestinal enzymes. The main route of exposure is through ingestion. In order to examine its resistance to digestion, we have applied a popular 1.0 INFOGEST protocol [1], specialized for the complete food, which in vitro mimics physiologically relevant conditions of oral-gastric-intestinal digestion. The aim of this study was to compare Cor a 8 resistance to gastric digestion, from both, raw and roasted hazelnuts, before and upon pepsin (gastric) digestion. Stability of the Cor a 8 protein was investigated by simulation of oral and gastric digestion phases, performed with ground raw and roasted hazelnut kernels. Hazelnut proteins were extracted from the digestion mixture and analyzed by 1D and 2D SDS-PAGE, while raw and roasted Cor a 8 western blots were probed with specific anti-Cor a 8 antibodies in 1D and 2D immunoblots. The electrophoretic patterns of the raw and roasted extracts were similar. 1D SDS PAGE profiles demonstrated high stability of Cor a 8 against enzymatic treatments. Control samples of Cor a 8 from raw and roasted hazelnut extracts migrated as a single band at around 12 kDa in 1D immunoblot. However, in case of roasted hazelnut, the protein showed a slightly lower capacity to bind specific anti-Cor a 8 antibody, as compared to raw hazelnut extract. In 2D immunoblot, with higher resolution, specific antibody binding was decting a significant and noticeable smear in the basic region indicating a range of different protein variants. This was more pronounced detectable in the case of roasted sample upon digestion, pointing to a mix of variants in this allergen batch. It has been suggested that the allergenicity of the Cor a 8 is almost insensitive to temperature. The allergen is stable even after digestion and roasting processes up to 140˚C. We hypothesize that a lipid-rich food matrix delays extraction of proteins, thereby delaying their gastrointestinal digestion, which may affect allergen sensitizing capacity and clinical symptoms.",
publisher = "Sociedade Portuguesa de Química",
journal = "Book of Abstracts of the XXI EuroFoodChem Congress",
title = "Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol",
pages = "126-126",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5762"
}
Prodić, I., Smiljanić, K., Nagl, C., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2021). Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol. in Book of Abstracts of the XXI EuroFoodChem Congress
Sociedade Portuguesa de Química., 126-126.
https://hdl.handle.net/21.15107/rcub_cherry_5762
Prodić I, Smiljanić K, Nagl C, Hoffmann-Sommergruber K, Ćirković-Veličković T. Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol. in Book of Abstracts of the XXI EuroFoodChem Congress. 2021;:126-126.
https://hdl.handle.net/21.15107/rcub_cherry_5762 .
Prodić, Ivana, Smiljanić, Katarina, Nagl, Christoph, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Allergenicity assessment of Cor a 8 from raw and roasted hazelnut upon oral-gastric digestion phase of INFOGEST protocol" in Book of Abstracts of the XXI EuroFoodChem Congress (2021):126-126,
https://hdl.handle.net/21.15107/rcub_cherry_5762 .

Methods Development for Protein and Modifications Profiling

Smiljanić, Katarina; Đukić, Teodora; Vasović, Tamara; Prodić, Ivana; Jovanović, Vesna; Ćirković-Veličković, Tanja

(Univerzitet u Beogradu - Hemijski fakultet, 2021)

TY  - CONF
AU  - Smiljanić, Katarina
AU  - Đukić, Teodora
AU  - Vasović, Tamara
AU  - Prodić, Ivana
AU  - Jovanović, Vesna
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5763
AB  - Post-translational modifications (PTMs) occur in many forms, and broadly influence protein behavior.
High-resolution tandem mass spectrometry coupled with engines for the identification of unspecified
PTMs, is a first-choice method for their global mapping. The significance of untargeted, in-depth PTM
profiling of various proteomes and its method development, just emerged, in contrast to proteomic studies
dealing with few selected static and dynamic modifications. In 2018, we have finalized our first study of
comprehensive analysis of multiple polluted and environmentally preserved Timothy grass pollen
samples that included novel method of relative quantification of proteins expressions and of open,
quantitative PTM profiling. It was among the first ones that has appeared in the proteomics field. In
addition to this, relative quantitative PTMs profiling of the raw and roasted peanut allergens was
completed in 2020, including validation of the method by specific antibodies. This peanut PTM study was
inspiration for the idea that porcine trypsin used in proteomic experiments can serve as a probe to
decipher differences in scissile bond hydrolysis caused by PTMs, with the steric and/or charge changes
causing possible hindrance or facilitation to its activity. We further hypothesized that effects observed
would be even more pronounced with human trypsin, since it is less efficient compared to the porcine
counterpart. Finally, we developed dual manual method to reassess our data of the major peanut allergen
Ara h 1 from the raw and roasted peanut, to confirm or rule out the first hypothesis (do PTMs positioned
on lysine/arginine residues facilitate or hinder porcine trypsin digestion efficacy). We believe that this
topic is relevant from the aspect of human gastrointestinal digestion of food allergens and PTMs
introduced by food processing. For further advancement in this area, novel algorithms based on deep
machine learning, capable of reporting cleavage and miscleavage events separately within unmodified
and modified part of protein sequences are warranted.
PB  - Univerzitet u Beogradu - Hemijski fakultet
C3  - Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021
T1  - Methods Development for Protein and Modifications Profiling
SP  - 11
EP  - 11
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5763
ER  - 
@conference{
author = "Smiljanić, Katarina and Đukić, Teodora and Vasović, Tamara and Prodić, Ivana and Jovanović, Vesna and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Post-translational modifications (PTMs) occur in many forms, and broadly influence protein behavior.
High-resolution tandem mass spectrometry coupled with engines for the identification of unspecified
PTMs, is a first-choice method for their global mapping. The significance of untargeted, in-depth PTM
profiling of various proteomes and its method development, just emerged, in contrast to proteomic studies
dealing with few selected static and dynamic modifications. In 2018, we have finalized our first study of
comprehensive analysis of multiple polluted and environmentally preserved Timothy grass pollen
samples that included novel method of relative quantification of proteins expressions and of open,
quantitative PTM profiling. It was among the first ones that has appeared in the proteomics field. In
addition to this, relative quantitative PTMs profiling of the raw and roasted peanut allergens was
completed in 2020, including validation of the method by specific antibodies. This peanut PTM study was
inspiration for the idea that porcine trypsin used in proteomic experiments can serve as a probe to
decipher differences in scissile bond hydrolysis caused by PTMs, with the steric and/or charge changes
causing possible hindrance or facilitation to its activity. We further hypothesized that effects observed
would be even more pronounced with human trypsin, since it is less efficient compared to the porcine
counterpart. Finally, we developed dual manual method to reassess our data of the major peanut allergen
Ara h 1 from the raw and roasted peanut, to confirm or rule out the first hypothesis (do PTMs positioned
on lysine/arginine residues facilitate or hinder porcine trypsin digestion efficacy). We believe that this
topic is relevant from the aspect of human gastrointestinal digestion of food allergens and PTMs
introduced by food processing. For further advancement in this area, novel algorithms based on deep
machine learning, capable of reporting cleavage and miscleavage events separately within unmodified
and modified part of protein sequences are warranted.",
publisher = "Univerzitet u Beogradu - Hemijski fakultet",
journal = "Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021",
title = "Methods Development for Protein and Modifications Profiling",
pages = "11-11",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5763"
}
Smiljanić, K., Đukić, T., Vasović, T., Prodić, I., Jovanović, V.,& Ćirković-Veličković, T.. (2021). Methods Development for Protein and Modifications Profiling. in Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021
Univerzitet u Beogradu - Hemijski fakultet., 11-11.
https://hdl.handle.net/21.15107/rcub_cherry_5763
Smiljanić K, Đukić T, Vasović T, Prodić I, Jovanović V, Ćirković-Veličković T. Methods Development for Protein and Modifications Profiling. in Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021. 2021;:11-11.
https://hdl.handle.net/21.15107/rcub_cherry_5763 .
Smiljanić, Katarina, Đukić, Teodora, Vasović, Tamara, Prodić, Ivana, Jovanović, Vesna, Ćirković-Veličković, Tanja, "Methods Development for Protein and Modifications Profiling" in Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021 (2021):11-11,
https://hdl.handle.net/21.15107/rcub_cherry_5763 .

Influence of Raw and Roasted Hazelnut Food Matrix on Ige Binding Activity After Application of the Harmonized Static Digestion Protocol

Prodić, Ivana; Smiljanić, Katarina; Hoffmann-Sommergruber, Karin; Ćirković-Veličković, Tanja

(Univerzitet u Beogradu - Hemijski fakultet, 2021)

TY  - CONF
AU  - Prodić, Ivana
AU  - Smiljanić, Katarina
AU  - Hoffmann-Sommergruber, Karin
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5764
AB  - Most of the hazelnut proteins are resistant to proteolysis in the gastrointestinal tract, and the survival
of their large fragments are essential for their sensitizing capacity. Usually, studies were carried out
on purified proteins, paying no attention to the potential impact of the food matrix and thermal
treatment on allergenicity. Obtained hazelnut peptides after gastric digestion, especially those with
potential IgE binding epitopes, highlight the need for further studies on their IgE reactivity. The aim
of this study was to investigate and compare digestion stability and allergenicity of large and small
peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under standardized
and physiologically relevant in vitro conditions, after thermal treatment (roasting as most abundant
type of thermal treatment). In vitro simulated oral and gastric phase digestion was carried out with
ground raw and roasted hazelnut kernels according to INFOGEST protocol. Digested proteins were
extracted from the digestion mixture and analysed by 1D and 2D SDS-PAGE, while their IgE biding
was probed with allergic patients’ sera via ELISA and 2D immunoblot. The most abundant hazelnut
allergens within 2DE map were acidic and basic chains of Cor a 9 and Cor a 11. Digestion-resistant
peptides of Cor a 11 and Cor a 9 were able to bind patients’ IgE. Roasted hazelnut is more prone to
gastric digestion than the raw sample, and cause milder IgE response in patients. Gastric phase
digestion of raw and roasted hazelnut kernels resulted in partial extraction and digestion of Cor a 11
and Cor a 9 into digestion-resistant peptides with preserved IgE-binding epitopes. These results
demonstrate substantial resistance of raw and roasted hazelnut allergens to gastric digestion since
they remained mostly intact after 2 h of gastric (pepsin) phase and retained their allergenicity.
PB  - Univerzitet u Beogradu - Hemijski fakultet
C3  - Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021, Belgrade 16-18 June
T1  - Influence of Raw and Roasted Hazelnut Food Matrix on Ige Binding Activity After Application of the Harmonized Static Digestion Protocol
SP  - 36
EP  - 36
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5764
ER  - 
@conference{
author = "Prodić, Ivana and Smiljanić, Katarina and Hoffmann-Sommergruber, Karin and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Most of the hazelnut proteins are resistant to proteolysis in the gastrointestinal tract, and the survival
of their large fragments are essential for their sensitizing capacity. Usually, studies were carried out
on purified proteins, paying no attention to the potential impact of the food matrix and thermal
treatment on allergenicity. Obtained hazelnut peptides after gastric digestion, especially those with
potential IgE binding epitopes, highlight the need for further studies on their IgE reactivity. The aim
of this study was to investigate and compare digestion stability and allergenicity of large and small
peptides released after pepsin digestion of whole raw and roasted hazelnut kernels under standardized
and physiologically relevant in vitro conditions, after thermal treatment (roasting as most abundant
type of thermal treatment). In vitro simulated oral and gastric phase digestion was carried out with
ground raw and roasted hazelnut kernels according to INFOGEST protocol. Digested proteins were
extracted from the digestion mixture and analysed by 1D and 2D SDS-PAGE, while their IgE biding
was probed with allergic patients’ sera via ELISA and 2D immunoblot. The most abundant hazelnut
allergens within 2DE map were acidic and basic chains of Cor a 9 and Cor a 11. Digestion-resistant
peptides of Cor a 11 and Cor a 9 were able to bind patients’ IgE. Roasted hazelnut is more prone to
gastric digestion than the raw sample, and cause milder IgE response in patients. Gastric phase
digestion of raw and roasted hazelnut kernels resulted in partial extraction and digestion of Cor a 11
and Cor a 9 into digestion-resistant peptides with preserved IgE-binding epitopes. These results
demonstrate substantial resistance of raw and roasted hazelnut allergens to gastric digestion since
they remained mostly intact after 2 h of gastric (pepsin) phase and retained their allergenicity.",
publisher = "Univerzitet u Beogradu - Hemijski fakultet",
journal = "Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021, Belgrade 16-18 June",
title = "Influence of Raw and Roasted Hazelnut Food Matrix on Ige Binding Activity After Application of the Harmonized Static Digestion Protocol",
pages = "36-36",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5764"
}
Prodić, I., Smiljanić, K., Hoffmann-Sommergruber, K.,& Ćirković-Veličković, T.. (2021). Influence of Raw and Roasted Hazelnut Food Matrix on Ige Binding Activity After Application of the Harmonized Static Digestion Protocol. in Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021, Belgrade 16-18 June
Univerzitet u Beogradu - Hemijski fakultet., 36-36.
https://hdl.handle.net/21.15107/rcub_cherry_5764
Prodić I, Smiljanić K, Hoffmann-Sommergruber K, Ćirković-Veličković T. Influence of Raw and Roasted Hazelnut Food Matrix on Ige Binding Activity After Application of the Harmonized Static Digestion Protocol. in Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021, Belgrade 16-18 June. 2021;:36-36.
https://hdl.handle.net/21.15107/rcub_cherry_5764 .
Prodić, Ivana, Smiljanić, Katarina, Hoffmann-Sommergruber, Karin, Ćirković-Veličković, Tanja, "Influence of Raw and Roasted Hazelnut Food Matrix on Ige Binding Activity After Application of the Harmonized Static Digestion Protocol" in Book of Abstracts of the Final 3rd Workshop FoodenTwin 2021, Belgrade 16-18 June (2021):36-36,
https://hdl.handle.net/21.15107/rcub_cherry_5764 .

Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability

Gligorijević, Nikola; Stanić-Vučinić, Dragana; Radomirović, Mirjana Ž.; Stojadinović, Marija M.; Khulal, Urmila; Nedić, Olgica; Ćirković-Veličković, Tanja

(MDPI, 2021)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana Ž.
AU  - Stojadinović, Marija M.
AU  - Khulal, Urmila
AU  - Nedić, Olgica
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://www.mdpi.com/1420-3049/26/10/2834
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4552
AB  - Resveratrol is a phytoalexin produced by many plants as a defense mechanism against stress-inducing conditions. The richest dietary sources of resveratrol are berries and grapes, their juices and wines. Good bioavailability of resveratrol is not reflected in its high biological activity in vivo because of resveratrol isomerization and its poor solubility in aqueous solutions. Proteins, cyclodextrins and nanomaterials have been explored as innovative delivery vehicles for resveratrol to overcome this limitation. Numerous in vitro and in vivo studies demonstrated beneficial effects of resveratrol in cardiovascular diseases (CVD). Main beneficial effects of resveratrol intake are cardioprotective, anti-hypertensive, vasodilatory, anti-diabetic, and improvement of lipid status. As resveratrol can alleviate the numerous factors associated with CVD, it has potential as a functional supplement to reduce COVID-19 illness severity in patients displaying poor prognosis due to cardio-vascular complications. Resveratrol was shown to mitigate the major pathways involved in the pathogenesis of SARS-CoV-2 including regulation of the renin-angiotensin system and expression of angiotensin-converting enzyme 2, stimulation of immune system and downregulation of pro-inflammatory cytokine release. Therefore, several studies already have anticipated potential implementation of resveratrol in COVID-19 treatment. Regular intake of a resveratrol rich diet, or resveratrol-based complementary medicaments, may contribute to a healthier cardio-vascular system, prevention and control of CVD, including COVID-19 disease related complications of CVD.
PB  - MDPI
T2  - Molecules
T1  - Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability
VL  - 26
IS  - 10
SP  - 2834
DO  - 10.3390/molecules26102834
ER  - 
@article{
author = "Gligorijević, Nikola and Stanić-Vučinić, Dragana and Radomirović, Mirjana Ž. and Stojadinović, Marija M. and Khulal, Urmila and Nedić, Olgica and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Resveratrol is a phytoalexin produced by many plants as a defense mechanism against stress-inducing conditions. The richest dietary sources of resveratrol are berries and grapes, their juices and wines. Good bioavailability of resveratrol is not reflected in its high biological activity in vivo because of resveratrol isomerization and its poor solubility in aqueous solutions. Proteins, cyclodextrins and nanomaterials have been explored as innovative delivery vehicles for resveratrol to overcome this limitation. Numerous in vitro and in vivo studies demonstrated beneficial effects of resveratrol in cardiovascular diseases (CVD). Main beneficial effects of resveratrol intake are cardioprotective, anti-hypertensive, vasodilatory, anti-diabetic, and improvement of lipid status. As resveratrol can alleviate the numerous factors associated with CVD, it has potential as a functional supplement to reduce COVID-19 illness severity in patients displaying poor prognosis due to cardio-vascular complications. Resveratrol was shown to mitigate the major pathways involved in the pathogenesis of SARS-CoV-2 including regulation of the renin-angiotensin system and expression of angiotensin-converting enzyme 2, stimulation of immune system and downregulation of pro-inflammatory cytokine release. Therefore, several studies already have anticipated potential implementation of resveratrol in COVID-19 treatment. Regular intake of a resveratrol rich diet, or resveratrol-based complementary medicaments, may contribute to a healthier cardio-vascular system, prevention and control of CVD, including COVID-19 disease related complications of CVD.",
publisher = "MDPI",
journal = "Molecules",
title = "Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability",
volume = "26",
number = "10",
pages = "2834",
doi = "10.3390/molecules26102834"
}
Gligorijević, N., Stanić-Vučinić, D., Radomirović, M. Ž., Stojadinović, M. M., Khulal, U., Nedić, O.,& Ćirković-Veličković, T.. (2021). Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability. in Molecules
MDPI., 26(10), 2834.
https://doi.org/10.3390/molecules26102834
Gligorijević N, Stanić-Vučinić D, Radomirović MŽ, Stojadinović MM, Khulal U, Nedić O, Ćirković-Veličković T. Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability. in Molecules. 2021;26(10):2834.
doi:10.3390/molecules26102834 .
Gligorijević, Nikola, Stanić-Vučinić, Dragana, Radomirović, Mirjana Ž., Stojadinović, Marija M., Khulal, Urmila, Nedić, Olgica, Ćirković-Veličković, Tanja, "Role of resveratrol in prevention and control of cardiovascular disorders and cardiovascular complications related to COVID-19 disease: Mode of action and approaches explored to increase its bioavailability" in Molecules, 26, no. 10 (2021):2834,
https://doi.org/10.3390/molecules26102834 . .
10
5
9

Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention

Gligorijevic, Nikola; Radomirović, Mirjana Ž.; Nedić, Olgica; Stojadinović, Marija M.; Khulal, Urmila; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(MDPI, 2021)

TY  - JOUR
AU  - Gligorijevic, Nikola
AU  - Radomirović, Mirjana Ž.
AU  - Nedić, Olgica
AU  - Stojadinović, Marija M.
AU  - Khulal, Urmila
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4784
AB  - The worldwide outbreak of COVID-19 was caused by a pathogenic virus called Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2). Therapies against SARS-CoV-2 target the virus or human cells or the immune system. However, therapies based on specific antibodies, such as vaccines and monoclonal antibodies, may become inefficient enough when the virus changes its antigenicity due to mutations. Polyphenols are the major class of bioactive compounds in nature, exerting diverse health effects based on their direct antioxidant activity and their effects in the modulation of intracellular signaling. There are currently numerous clinical trials investigating the effects of polyphenols in prophylaxis and the treatment of COVID-19, from symptomatic, via moderate and severe COVID-19 treatment, to anti-fibrotic treatment in discharged COVID-19 patients. Antiviral activities of polyphenols and their impact on immune system modulation could serve as a solid basis for developing polyphenol-based natural approaches for preventing and treating COVID-19.
PB  - MDPI
T2  - International Journal of Molecular Sciences
T1  - Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention
VL  - 22
IS  - 22
SP  - 12385
DO  - 10.3390/ijms222212385
ER  - 
@article{
author = "Gligorijevic, Nikola and Radomirović, Mirjana Ž. and Nedić, Olgica and Stojadinović, Marija M. and Khulal, Urmila and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "The worldwide outbreak of COVID-19 was caused by a pathogenic virus called Severe Acute Respiratory Syndrome Coronavirus-2 (SARS-CoV-2). Therapies against SARS-CoV-2 target the virus or human cells or the immune system. However, therapies based on specific antibodies, such as vaccines and monoclonal antibodies, may become inefficient enough when the virus changes its antigenicity due to mutations. Polyphenols are the major class of bioactive compounds in nature, exerting diverse health effects based on their direct antioxidant activity and their effects in the modulation of intracellular signaling. There are currently numerous clinical trials investigating the effects of polyphenols in prophylaxis and the treatment of COVID-19, from symptomatic, via moderate and severe COVID-19 treatment, to anti-fibrotic treatment in discharged COVID-19 patients. Antiviral activities of polyphenols and their impact on immune system modulation could serve as a solid basis for developing polyphenol-based natural approaches for preventing and treating COVID-19.",
publisher = "MDPI",
journal = "International Journal of Molecular Sciences",
title = "Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention",
volume = "22",
number = "22",
pages = "12385",
doi = "10.3390/ijms222212385"
}
Gligorijevic, N., Radomirović, M. Ž., Nedić, O., Stojadinović, M. M., Khulal, U., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention. in International Journal of Molecular Sciences
MDPI., 22(22), 12385.
https://doi.org/10.3390/ijms222212385
Gligorijevic N, Radomirović MŽ, Nedić O, Stojadinović MM, Khulal U, Stanić-Vučinić D, Ćirković-Veličković T. Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention. in International Journal of Molecular Sciences. 2021;22(22):12385.
doi:10.3390/ijms222212385 .
Gligorijevic, Nikola, Radomirović, Mirjana Ž., Nedić, Olgica, Stojadinović, Marija M., Khulal, Urmila, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Molecular Mechanisms of Possible Action of Phenolic Compounds in COVID-19 Protection and Prevention" in International Journal of Molecular Sciences, 22, no. 22 (2021):12385,
https://doi.org/10.3390/ijms222212385 . .
1
5
6

Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying

Peruško, Marija; Ghnimi, Sami; Simović, Ana; Stevanović, Nikola R.; Radomirović, Mirjana Ž.; Gharsallaoui, Adem; Smiljanić, Katarina; Van Haute, Sam; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - JOUR
AU  - Peruško, Marija
AU  - Ghnimi, Sami
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Radomirović, Mirjana Ž.
AU  - Gharsallaoui, Adem
AU  - Smiljanić, Katarina
AU  - Van Haute, Sam
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4332
AB  - Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.
PB  - Elsevier
T2  - LWT
T1  - Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying
VL  - 143
SP  - 111091
DO  - 10.1016/j.lwt.2021.111091
ER  - 
@article{
author = "Peruško, Marija and Ghnimi, Sami and Simović, Ana and Stevanović, Nikola R. and Radomirović, Mirjana Ž. and Gharsallaoui, Adem and Smiljanić, Katarina and Van Haute, Sam and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.",
publisher = "Elsevier",
journal = "LWT",
title = "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying",
volume = "143",
pages = "111091",
doi = "10.1016/j.lwt.2021.111091"
}
Peruško, M., Ghnimi, S., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Gharsallaoui, A., Smiljanić, K., Van Haute, S., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT
Elsevier., 143, 111091.
https://doi.org/10.1016/j.lwt.2021.111091
Peruško M, Ghnimi S, Simović A, Stevanović NR, Radomirović MŽ, Gharsallaoui A, Smiljanić K, Van Haute S, Stanić-Vučinić D, Ćirković-Veličković T. Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT. 2021;143:111091.
doi:10.1016/j.lwt.2021.111091 .
Peruško, Marija, Ghnimi, Sami, Simović, Ana, Stevanović, Nikola R., Radomirović, Mirjana Ž., Gharsallaoui, Adem, Smiljanić, Katarina, Van Haute, Sam, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying" in LWT, 143 (2021):111091,
https://doi.org/10.1016/j.lwt.2021.111091 . .
1
10
2
10

Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying

Peruško, Marija; Ghnimi, Sami; Simović, Ana; Stevanović, Nikola R.; Radomirović, Mirjana Ž.; Gharsallaoui, Adem; Smiljanić, Katarina; Van Haute, Sam; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - JOUR
AU  - Peruško, Marija
AU  - Ghnimi, Sami
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Radomirović, Mirjana Ž.
AU  - Gharsallaoui, Adem
AU  - Smiljanić, Katarina
AU  - Van Haute, Sam
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4333
AB  - Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.
PB  - Elsevier
T2  - LWT
T1  - Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying
VL  - 143
SP  - 111091
DO  - 10.1016/j.lwt.2021.111091
ER  - 
@article{
author = "Peruško, Marija and Ghnimi, Sami and Simović, Ana and Stevanović, Nikola R. and Radomirović, Mirjana Ž. and Gharsallaoui, Adem and Smiljanić, Katarina and Van Haute, Sam and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Demand for camel milk (CM) is increasing worldwide, due to its high nutritious value and health benefits. In this study, whole CM powders were produced by spray drying (SD) at six inlet temperatures (190 °C–250 °C) and by freeze drying (FD). Physicochemical and functional properties of CM powder proteins were investigated. SD at higher inlet temperatures (230 °C–250 °C) resulted in higher extent of Maillard reaction (MR), in comparison to lower temperatures (190 °C–200 °C) and FD treatment. Both treatments had negative effect on casein solubility, while whey proteins remained soluble and slightly increased its solubility with the extent of MR. The CM powders obtained at higher inlet temperatures demonstrated improved antioxidant activity. Secondary structure of whey proteins did not differ among the samples, while surface hydrophobicity of whey proteins was higher in all SD than in FD samples, suggesting only limited denaturation of camel whey proteins at higher inlet temperatures of drying. Thus, the effects of SD under the conditions applied in our study did not decrease camel whey protein solubility, while drying procedure itself regardless of temperature decreased solubility of camel milk caseins. MR generated during CM processing could be an important means of compensating for the lack of antioxidant protection normally associated with β-lactoglobulin but happens to be absent from this milk.",
publisher = "Elsevier",
journal = "LWT",
title = "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying",
volume = "143",
pages = "111091",
doi = "10.1016/j.lwt.2021.111091"
}
Peruško, M., Ghnimi, S., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Gharsallaoui, A., Smiljanić, K., Van Haute, S., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT
Elsevier., 143, 111091.
https://doi.org/10.1016/j.lwt.2021.111091
Peruško M, Ghnimi S, Simović A, Stevanović NR, Radomirović MŽ, Gharsallaoui A, Smiljanić K, Van Haute S, Stanić-Vučinić D, Ćirković-Veličković T. Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying. in LWT. 2021;143:111091.
doi:10.1016/j.lwt.2021.111091 .
Peruško, Marija, Ghnimi, Sami, Simović, Ana, Stevanović, Nikola R., Radomirović, Mirjana Ž., Gharsallaoui, Adem, Smiljanić, Katarina, Van Haute, Sam, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Maillard reaction products formation and antioxidative power of spray dried camel milk powders increases with the inlet temperature of drying" in LWT, 143 (2021):111091,
https://doi.org/10.1016/j.lwt.2021.111091 . .
1
10
2
10

Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.

Peruško, Marija; Ghnimi, Sami; Simović, Ana; Stevanović, Nikola R.; Radomirović, Mirjana Ž.; Gharsallaoui, Adem; Smiljanić, Katarina; Van Haute, Sam; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier, 2021)

TY  - DATA
AU  - Peruško, Marija
AU  - Ghnimi, Sami
AU  - Simović, Ana
AU  - Stevanović, Nikola R.
AU  - Radomirović, Mirjana Ž.
AU  - Gharsallaoui, Adem
AU  - Smiljanić, Katarina
AU  - Van Haute, Sam
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4334
PB  - Elsevier
T2  - LWT
T1  - Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4334
ER  - 
@misc{
author = "Peruško, Marija and Ghnimi, Sami and Simović, Ana and Stevanović, Nikola R. and Radomirović, Mirjana Ž. and Gharsallaoui, Adem and Smiljanić, Katarina and Van Haute, Sam and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
publisher = "Elsevier",
journal = "LWT",
title = "Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4334"
}
Peruško, M., Ghnimi, S., Simović, A., Stevanović, N. R., Radomirović, M. Ž., Gharsallaoui, A., Smiljanić, K., Van Haute, S., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.. in LWT
Elsevier..
https://hdl.handle.net/21.15107/rcub_cherry_4334
Peruško M, Ghnimi S, Simović A, Stevanović NR, Radomirović MŽ, Gharsallaoui A, Smiljanić K, Van Haute S, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091.. in LWT. 2021;.
https://hdl.handle.net/21.15107/rcub_cherry_4334 .
Peruško, Marija, Ghnimi, Sami, Simović, Ana, Stevanović, Nikola R., Radomirović, Mirjana Ž., Gharsallaoui, Adem, Smiljanić, Katarina, Van Haute, Sam, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Supplementary data for the article: Perusko, M.; Ghnimi, S.; Simovic, A.; Stevanovic, N.; Radomirovic, M.; Gharsallaoui, A.; Smiljanic, K.; Van Haute, S.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Maillard Reaction Products Formation and Antioxidative Power of Spray Dried Camel Milk Powders Increases with the Inlet Temperature of Drying. LWT 2021, 143, 111091. https://doi.org/10.1016/j.lwt.2021.111091." in LWT (2021),
https://hdl.handle.net/21.15107/rcub_cherry_4334 .

Ligand binding to fibrinogen influences its structure and function

Gligorijević, Nikola; Minić, Simeon L.; Radomirović, Mirjana Ž.; Lević, Steva M.; Nikolić, Milan; Ćirković-Veličković, Tanja; Nedić, Olgica

(University of Novi Sad - Faculty of Sciences, Department of Biology, 2021)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Lević, Steva M.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
AU  - Nedić, Olgica
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4862
AB  - Fibrinogen is a plasma protein that is highly susceptible to oxidation. Because of this chemical modification, fibrinogen acquires thrombogenic characteristics under different pathophysiological conditions. Increased carbonyl content and reduced porosity impair the degradation of formed fibrin mediated by plasmin. Fibrinogen is capable of interacting with many proteins, ions, and small molecules. These interactions can modify the functions of this protein. The discovery of new binding partners that may protect fibrinogen from harmful oxidation and, thus, preserve its normal function is essential. Some of the newly detected interactions between fibrinogen and small, natural bioactive molecules, together with the influence of these interactions on the structure and function of fibrinogen, will be presented in this text.
PB  - University of Novi Sad - Faculty of Sciences, Department of Biology
T2  - Biologia Serbica
T1  - Ligand binding to fibrinogen influences its structure and function
VL  - 43
IS  - 1
DO  - 10.5281/zenodo.5512285
ER  - 
@article{
author = "Gligorijević, Nikola and Minić, Simeon L. and Radomirović, Mirjana Ž. and Lević, Steva M. and Nikolić, Milan and Ćirković-Veličković, Tanja and Nedić, Olgica",
year = "2021",
abstract = "Fibrinogen is a plasma protein that is highly susceptible to oxidation. Because of this chemical modification, fibrinogen acquires thrombogenic characteristics under different pathophysiological conditions. Increased carbonyl content and reduced porosity impair the degradation of formed fibrin mediated by plasmin. Fibrinogen is capable of interacting with many proteins, ions, and small molecules. These interactions can modify the functions of this protein. The discovery of new binding partners that may protect fibrinogen from harmful oxidation and, thus, preserve its normal function is essential. Some of the newly detected interactions between fibrinogen and small, natural bioactive molecules, together with the influence of these interactions on the structure and function of fibrinogen, will be presented in this text.",
publisher = "University of Novi Sad - Faculty of Sciences, Department of Biology",
journal = "Biologia Serbica",
title = "Ligand binding to fibrinogen influences its structure and function",
volume = "43",
number = "1",
doi = "10.5281/zenodo.5512285"
}
Gligorijević, N., Minić, S. L., Radomirović, M. Ž., Lević, S. M., Nikolić, M., Ćirković-Veličković, T.,& Nedić, O.. (2021). Ligand binding to fibrinogen influences its structure and function. in Biologia Serbica
University of Novi Sad - Faculty of Sciences, Department of Biology., 43(1).
https://doi.org/10.5281/zenodo.5512285
Gligorijević N, Minić SL, Radomirović MŽ, Lević SM, Nikolić M, Ćirković-Veličković T, Nedić O. Ligand binding to fibrinogen influences its structure and function. in Biologia Serbica. 2021;43(1).
doi:10.5281/zenodo.5512285 .
Gligorijević, Nikola, Minić, Simeon L., Radomirović, Mirjana Ž., Lević, Steva M., Nikolić, Milan, Ćirković-Veličković, Tanja, Nedić, Olgica, "Ligand binding to fibrinogen influences its structure and function" in Biologia Serbica, 43, no. 1 (2021),
https://doi.org/10.5281/zenodo.5512285 . .

Interaction of SARS-CoV-2 Spike protein with phycocyanobilin

Simović, Ana; Radomirović, Mirjana Ž.; Gligorijević, Nikola; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Sociedade Portuguesa de Química, 2021)

TY  - CONF
AU  - Simović, Ana
AU  - Radomirović, Mirjana Ž.
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5132
AB  - Algae have been consumed as food and medicine for centuries. Their benefits are so pronounced, due to high concentrations of vitamins, minerals, antioxidants and proteins that they are commonly referred to as superfoods. Phycocyanobilin (PCB) is a bioactive compound of microalga Spirulina platensis. It is a blue tetrapyrrole chromophore of C-phycocyanin (C-PC), the major chromoprotein of this microalga. It is covalently attached to cysteine residues of C-PC via thioether bond. The outbreak of Coronavirus Disease 2019 (COVID-19) has posed a serious threat to global public health, calling for the development of safe and effective prophylactics and therapeutics against infection of its causative agent, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The SARS-CoV-2 spike (S) protein plays the most important roles in viral attachment, fusion and entry, and it serves as a target for development of antibodies, entry inhibitors and vaccines. It mediates viral entry into host cells by first binding to a host angiotensin-converting enzyme 2 (ACE2) receptor through the receptor-binding domain (RBD) and then fusing the viral and host membranes. This study aimed to investigate interaction of bioactive PCB with S protein and RBD respectively.
Combination of electrophoretic techniques and fluorescence spectroscopy was employed in order to examine interactions of PCB and S protein, as well as interactions of PCB 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 fluorescence quenching method were: 2.1 x 107 M–1 for PCB and S protein, and 8.4 x 104 M–1 for PCB and RBD. Far-UV circular dichroism spectra showed that PCB influences RBD structure.
Our results support the importance of further research on covalent binding of PCB to S protein and RBD and its implications. Due to its interaction with S protein and RBD, PCB may exert one of its many bioactive effects via impact on S protein binding to ACE2 receptor.
Acknowledgments: This project has received funding from the European Union’s Horizon 2020 research and innovation program under grant agreement No. 810752.
References:
[1] S. Minic, M. Radomirovic, N. Savkovic et al., Food Chemistry, 269(2018) 43-52.
[2] W. Tai, L. He, X. Zhang et al., Cellular & Molecular Immunology, 17(2020) 613-620.
PB  - Sociedade Portuguesa de Química
C3  - Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference
T1  - Interaction of SARS-CoV-2 Spike protein with phycocyanobilin
SP  - 164
EP  - 164
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5132
ER  - 
@conference{
author = "Simović, Ana and Radomirović, Mirjana Ž. and Gligorijević, Nikola and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Algae have been consumed as food and medicine for centuries. Their benefits are so pronounced, due to high concentrations of vitamins, minerals, antioxidants and proteins that they are commonly referred to as superfoods. Phycocyanobilin (PCB) is a bioactive compound of microalga Spirulina platensis. It is a blue tetrapyrrole chromophore of C-phycocyanin (C-PC), the major chromoprotein of this microalga. It is covalently attached to cysteine residues of C-PC via thioether bond. The outbreak of Coronavirus Disease 2019 (COVID-19) has posed a serious threat to global public health, calling for the development of safe and effective prophylactics and therapeutics against infection of its causative agent, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The SARS-CoV-2 spike (S) protein plays the most important roles in viral attachment, fusion and entry, and it serves as a target for development of antibodies, entry inhibitors and vaccines. It mediates viral entry into host cells by first binding to a host angiotensin-converting enzyme 2 (ACE2) receptor through the receptor-binding domain (RBD) and then fusing the viral and host membranes. This study aimed to investigate interaction of bioactive PCB with S protein and RBD respectively.
Combination of electrophoretic techniques and fluorescence spectroscopy was employed in order to examine interactions of PCB and S protein, as well as interactions of PCB 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 fluorescence quenching method were: 2.1 x 107 M–1 for PCB and S protein, and 8.4 x 104 M–1 for PCB and RBD. Far-UV circular dichroism spectra showed that PCB influences RBD structure.
Our results support the importance of further research on covalent binding of PCB to S protein and RBD and its implications. Due to its interaction with S protein and RBD, PCB may exert one of its many bioactive effects via impact on S protein binding to ACE2 receptor.
Acknowledgments: This project has received funding from the European Union’s Horizon 2020 research and innovation program under grant agreement No. 810752.
References:
[1] S. Minic, M. Radomirovic, N. Savkovic et al., Food Chemistry, 269(2018) 43-52.
[2] W. Tai, L. He, X. Zhang et al., Cellular & Molecular Immunology, 17(2020) 613-620.",
publisher = "Sociedade Portuguesa de Química",
journal = "Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference",
title = "Interaction of SARS-CoV-2 Spike protein with phycocyanobilin",
pages = "164-164",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5132"
}
Simović, A., Radomirović, M. Ž., Gligorijević, N., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2021). Interaction of SARS-CoV-2 Spike protein with phycocyanobilin. in Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference
Sociedade Portuguesa de Química., 164-164.
https://hdl.handle.net/21.15107/rcub_cherry_5132
Simović A, Radomirović MŽ, Gligorijević N, Stanić-Vučinić D, Ćirković-Veličković T. Interaction of SARS-CoV-2 Spike protein with phycocyanobilin. in Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference. 2021;:164-164.
https://hdl.handle.net/21.15107/rcub_cherry_5132 .
Simović, Ana, Radomirović, Mirjana Ž., Gligorijević, Nikola, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Interaction of SARS-CoV-2 Spike protein with phycocyanobilin" in Book of Abstracts of the XXI EuroFoodChem Congress, 22-24 November 2021, On-line conference (2021):164-164,
https://hdl.handle.net/21.15107/rcub_cherry_5132 .

Proteomic and immunological characterization of recombinantly expressed nucleocapsid SARS-CoV 2 protein fragment in E. coli

Đukić, Teodora; Mladenović, Maja; Stanić-Vučinić, Dragana; Radosavljević, Jelena; Smiljanić, Katarina; Sabljić, Ljiljana; Gnjatović, Marija Lj.; Cujić, Danica; Vasović, Tamara; Simović, Ana; Radomirović, Mirjana Ž.; Ćirković-Veličković, Tanja

(2021)

TY  - CONF
AU  - Đukić, Teodora
AU  - Mladenović, Maja
AU  - Stanić-Vučinić, Dragana
AU  - Radosavljević, Jelena
AU  - Smiljanić, Katarina
AU  - Sabljić, Ljiljana
AU  - Gnjatović, Marija Lj.
AU  - Cujić, Danica
AU  - Vasović, Tamara
AU  - Simović, Ana
AU  - Radomirović, Mirjana Ž.
AU  - Ćirković-Veličković, Tanja
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5735
AB  - Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARSCoV-2) infection and for assessment of immunological response after the vaccination. Nucleocapsid (N) protein is the most abundant virus protein and strong immunogen. The aim was develop efficient, low-cost production of N protein large fragment and to characterize it with bottom-up, high-resolution tandem mass spectrometry and immunologically.
SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form and purified by several chromatographic steps and was subjected to SDS-PAGE and in-gel digested with trypsin.
rfNP was tested in immunoblot using sera of COVID-19 convalescent patients. 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. Identity of rfNP was confirmed with high scores and peptide coverage above 80%. Estimation from the value of areas under ion extracted chromatographic curves is that only up to 0,03% of the total band protein quantity belongs to host proteins, while rfNP share is well above 99,9%, resulting in highly pure nucleocapsid protein preparation.
C3  - Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021
T1  - Proteomic and immunological characterization of recombinantly expressed nucleocapsid SARS-CoV 2 protein fragment in E. coli
SP  - 50
EP  - 50
UR  - https://hdl.handle.net/21.15107/rcub_cherry_5735
ER  - 
@conference{
author = "Đukić, Teodora and Mladenović, Maja and Stanić-Vučinić, Dragana and Radosavljević, Jelena and Smiljanić, Katarina and Sabljić, Ljiljana and Gnjatović, Marija Lj. and Cujić, Danica and Vasović, Tamara and Simović, Ana and Radomirović, Mirjana Ž. and Ćirković-Veličković, Tanja",
year = "2021",
abstract = "Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARSCoV-2) infection and for assessment of immunological response after the vaccination. Nucleocapsid (N) protein is the most abundant virus protein and strong immunogen. The aim was develop efficient, low-cost production of N protein large fragment and to characterize it with bottom-up, high-resolution tandem mass spectrometry and immunologically.
SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form and purified by several chromatographic steps and was subjected to SDS-PAGE and in-gel digested with trypsin.
rfNP was tested in immunoblot using sera of COVID-19 convalescent patients. 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. Identity of rfNP was confirmed with high scores and peptide coverage above 80%. Estimation from the value of areas under ion extracted chromatographic curves is that only up to 0,03% of the total band protein quantity belongs to host proteins, while rfNP share is well above 99,9%, resulting in highly pure nucleocapsid protein preparation.",
journal = "Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021",
title = "Proteomic and immunological characterization of recombinantly expressed nucleocapsid SARS-CoV 2 protein fragment in E. coli",
pages = "50-50",
url = "https://hdl.handle.net/21.15107/rcub_cherry_5735"
}
Đukić, T., Mladenović, M., Stanić-Vučinić, D., Radosavljević, J., Smiljanić, K., Sabljić, L., Gnjatović, M. Lj., Cujić, D., Vasović, T., Simović, A., Radomirović, M. Ž.,& Ćirković-Veličković, T.. (2021). Proteomic and immunological characterization of recombinantly expressed nucleocapsid SARS-CoV 2 protein fragment in E. coli. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021, 50-50.
https://hdl.handle.net/21.15107/rcub_cherry_5735
Đukić T, Mladenović M, Stanić-Vučinić D, Radosavljević J, Smiljanić K, Sabljić L, Gnjatović ML, Cujić D, Vasović T, Simović A, Radomirović MŽ, Ćirković-Veličković T. Proteomic and immunological characterization of recombinantly expressed nucleocapsid SARS-CoV 2 protein fragment in E. coli. in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021. 2021;:50-50.
https://hdl.handle.net/21.15107/rcub_cherry_5735 .
Đukić, Teodora, Mladenović, Maja, Stanić-Vučinić, Dragana, Radosavljević, Jelena, Smiljanić, Katarina, Sabljić, Ljiljana, Gnjatović, Marija Lj., Cujić, Danica, Vasović, Tamara, Simović, Ana, Radomirović, Mirjana Ž., Ćirković-Veličković, Tanja, "Proteomic and immunological characterization of recombinantly expressed nucleocapsid SARS-CoV 2 protein fragment in E. coli" in Proteomics and Metabolomics for Personalized Medicine, XV Italian Proteomics Association Annual Meeting, Catholic University of the Sacred Heart, Roma, Italy, 8th-10th September 2021 (2021):50-50,
https://hdl.handle.net/21.15107/rcub_cherry_5735 .