Ćirković-Veličković, Tanja

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Authority KeyName Variants
orcid::0000-0003-2559-5234
  • Ćirković-Veličković, Tanja (215)
Projects
Molecular properties and modifications of some respiratory and nutritional allergens Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research
FoodEnTwin-Twinning of research activities for the frontier research in the fields of food, nutrition and environmental omics Ispitivanje strukture i funkcije biološki važnih makromolekula u fiziološkim i patološkim stanjima
Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200168 (University of Belgrade, Faculty of Chemistry) Swedish Research Council
King Gustaf V 80th Birthday Foundation Magnus Bergvall Foundation
Swedish Asthma and Allergy Associations Research Foundation Swedish Cancer and Allergy Foundation
Swedish Heart-Lung Foundation Stockholm County Council
Hesselman Foundation Allergens, antibodies, enzymes and small physiologically important molecules: design, structure, function and relevance
Karolinska Institutet Rational design and synthesis of biologically active and coordination compounds and functional materials, relevant for (bio)nanotechnology
Swedish Association for Allergology Center for Inflammatory Diseases
Application of advanced oxidation processes and nanostructured oxide materials for the removal of pollutants from the environment, development and optimisation of instrumental techniques for efficiency monitoring Serbian Academy of Sciences and Arts GA No. F-26.
Serbian Academy of Sciences and Arts Project F-26. Austrian Science Fund (FWF) [F4605]
COST Action [FA 1005] EAACI
EAACI Fellowship Award Ghent University Global Campus, Belgian Special Research Fund BOF StG No. 01N01718.
Structure-properties relationships of natural and synthetic molecules and their metal complexes Structural characterisation of the insulin-like growth factor (IGF) binding proteins and IGF receptors, their interactions with other physiological molecules and alterations in metabolic disorders
Ministry of Education, Science and Technological Development, Republic of Serbia, Grant no. 451-03-68/2020-14/200288 (Innovation Center of the Faculty of Chemistry) The European Union's Horizon 2020 Research and Innovation Program—ID‐LYME GA No. 720480.

Author's Bibliography

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; Stojadinović, Marija M.; Khulal, Urmila; Nedić, Olgica; Ćirković-Veličković, Tanja

(MDPI, 2021)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana
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  - http://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 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., 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 M, 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, 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 . .
1
2

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, 2021)

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  - 2021
UR  - http://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
SP  - 1
EP  - 17
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 = "2021",
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",
pages = "1-17",
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.. (2021). New applications of advanced instrumental techniques for the characterization of food allergenic proteins. in Critical Reviews in Food Science and Nutrition
Taylor & Francis Group., 1-17.
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. 2021;:1-17.
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 (2021):1-17,
https://doi.org/10.1080/10408398.2021.1931806 . .
1

Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2

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

(Elsevier, 2021)

TY  - JOUR
AU  - Đukić, Teodora
AU  - Mladenović, Maja
AU  - Stanić-Vučinić, Dragana
AU  - Radosavljević, Jelena
AU  - Smiljanić, Katarina
AU  - Sabljić, Ljiljana
AU  - Dević, Marija
AU  - Ćujić, 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/123456789/4330
AB  - Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production.

SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified and characterized biochemically and immunologically.

Purified rfNP has secondary structure of full-length recombinant N protein, with high percentage of disordered structure (34.2%) and of β-sheet (40.7%). 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 (94% and 96.5%, respectively).

Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection.
PB  - Elsevier
T2  - Virology journal
T1  - Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2
VL  - 557
SP  - 15
EP  - 22
DO  - 10.1016/j.virol.2021.01.004
ER  - 
@article{
author = "Đukić, Teodora and Mladenović, Maja and Stanić-Vučinić, Dragana and Radosavljević, Jelena and Smiljanić, Katarina and Sabljić, Ljiljana and Dević, Marija and Ćujić, 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 (SARS-CoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production.

SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified and characterized biochemically and immunologically.

Purified rfNP has secondary structure of full-length recombinant N protein, with high percentage of disordered structure (34.2%) and of β-sheet (40.7%). 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 (94% and 96.5%, respectively).

Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection.",
publisher = "Elsevier",
journal = "Virology journal",
title = "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2",
volume = "557",
pages = "15-22",
doi = "10.1016/j.virol.2021.01.004"
}
Đukić, T., Mladenović, M., Stanić-Vučinić, D., Radosavljević, J., Smiljanić, K., Sabljić, L., Dević, M., Ćujić, D., Vasović, T., Simović, A., Radomirović, M. Ž.,& Ćirković-Veličković, T.. (2021). Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2. in Virology journal
Elsevier., 557, 15-22.
https://doi.org/10.1016/j.virol.2021.01.004
Đukić T, Mladenović M, Stanić-Vučinić D, Radosavljević J, Smiljanić K, Sabljić L, Dević M, Ćujić D, Vasović T, Simović A, Radomirović MŽ, Ćirković-Veličković T. Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2. in Virology journal. 2021;557:15-22.
doi:10.1016/j.virol.2021.01.004 .
Đukić, Teodora, Mladenović, Maja, Stanić-Vučinić, Dragana, Radosavljević, Jelena, Smiljanić, Katarina, Sabljić, Ljiljana, Dević, Marija, Ćujić, Danica, Vasović, Tamara, Simović, Ana, Radomirović, Mirjana Ž., Ćirković-Veličković, Tanja, "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2" in Virology journal, 557 (2021):15-22,
https://doi.org/10.1016/j.virol.2021.01.004 . .
6
2
1

Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2

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

(Elsevier, 2021)

TY  - JOUR
AU  - Đukić, Teodora
AU  - Mladenović, Maja
AU  - Stanić-Vučinić, Dragana
AU  - Radosavljević, Jelena
AU  - Smiljanić, Katarina
AU  - Sabljić, Ljiljana
AU  - Dević, Marija
AU  - Ćujić, 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/123456789/4331
AB  - Serological testing is important method for diagnosis of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production.SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified and characterized biochemically and immunologically.Purified rfNP has secondary structure of full-length recombinant N protein, with high percentage of disordered structure (34.2%) and of β-sheet (40.7%). 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 (94% and 96.5%, respectively).Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection.
PB  - Elsevier
T2  - Virology journal
T1  - Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2
VL  - 557
SP  - 15
EP  - 22
DO  - 10.1016/j.virol.2021.01.004
ER  - 
@article{
author = "Đukić, Teodora and Mladenović, Maja and Stanić-Vučinić, Dragana and Radosavljević, Jelena and Smiljanić, Katarina and Sabljić, Ljiljana and Dević, Marija and Ćujić, 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 (SARS-CoV-2) infection. Nucleocapsid (N) protein is the most abundant virus derived protein and strong immunogen. We aimed to find its efficient, low-cost production.SARS-CoV-2 recombinant fragment of nucleocapsid protein (rfNP; 58–419 aa) was expressed in E. coli in soluble form, purified and characterized biochemically and immunologically.Purified rfNP has secondary structure of full-length recombinant N protein, with high percentage of disordered structure (34.2%) and of β-sheet (40.7%). 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 (94% and 96.5%, respectively).Cost-effective approach for soluble recombinant N protein fragment production was developed, with reliable IgG and IgM antibodies detection of SARS-CoV-2 infection.",
publisher = "Elsevier",
journal = "Virology journal",
title = "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2",
volume = "557",
pages = "15-22",
doi = "10.1016/j.virol.2021.01.004"
}
Đukić, T., Mladenović, M., Stanić-Vučinić, D., Radosavljević, J., Smiljanić, K., Sabljić, L., Dević, M., Ćujić, D., Vasović, T., Simović, A., Radomirović, M. Ž.,& Ćirković-Veličković, T.. (2021). Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2. in Virology journal
Elsevier., 557, 15-22.
https://doi.org/10.1016/j.virol.2021.01.004
Đukić T, Mladenović M, Stanić-Vučinić D, Radosavljević J, Smiljanić K, Sabljić L, Dević M, Ćujić D, Vasović T, Simović A, Radomirović MŽ, Ćirković-Veličković T. Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2. in Virology journal. 2021;557:15-22.
doi:10.1016/j.virol.2021.01.004 .
Đukić, Teodora, Mladenović, Maja, Stanić-Vučinić, Dragana, Radosavljević, Jelena, Smiljanić, Katarina, Sabljić, Ljiljana, Dević, Marija, Ćujić, Danica, Vasović, Tamara, Simović, Ana, Radomirović, Mirjana Ž., Ćirković-Veličković, Tanja, "Expression, purification and immunological characterization of recombinant nucleocapsid protein fragment from SARS-CoV-2" in Virology journal, 557 (2021):15-22,
https://doi.org/10.1016/j.virol.2021.01.004 . .
6
2
1

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  - http://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
2
2

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  - http://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
2
2

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  - http://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.
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."
}
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..
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;..
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).

Interaction, binding capacity and anticancer properties of N,N′-bis(acetylacetone)-propylenediimine-copper(II) on colorectal cancer cell line Caco-2

Stevanović, Nikola R.; Apostolović, Danijela; Milčić, Miloš K.; Lolić, Aleksandar; Hage, Marianne van; Ćirković-Veličković, Tanja; Baošić, Rada

(2021)

TY  - JOUR
AU  - Stevanović, Nikola R.
AU  - Apostolović, Danijela
AU  - Milčić, Miloš K.
AU  - Lolić, Aleksandar
AU  - Hage, Marianne van
AU  - Ćirković-Veličković, Tanja
AU  - Baošić, Rada
PY  - 2021
UR  - https://pubs.rsc.org/en/content/articlelanding/2021/nj/d1nj00040c
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4399
AB  - Different Schiff base complexes have biological activities that make them suitable for drug design. The biological properties of tetradentate Schiff base copper(II) complexed with N,N′-bis(acetylacetone)propylenediimine have been studied. The cytotoxic activity towards Caco-2 cells were determined by MTT, Anexin V and PI apoptosis assays. N,N′-bis(acetylacetone)propylenediimine-copper(II) showed the anti-cancer and anti-proliferative properties by inducing apoptosis in Caco-2 cells. A comparison of the cytotoxic activity of this compound with cisplatin shows that it is more effective on the colorectal cancer cell line Caco-2. The binding capacity and interaction of N,N′-bis(acetylacetone)propylenediimine-copper(II) with HSA were systemically investigated by in vitro fluorescence spectroscopy, CD spectroscopy, and in silico molecular docking study. Furthermore, in vitro and in silico interaction studies indicated that the complex binds to HSA through a static quenching mechanism without changes in protein conformation. The calculated number of binding sites was in line with molecular docking studies. The obtained Ka value suggests that the compound can be released from the protein in target cells. The tetradentate Schiff base copper(II) complex exhibited in vitro biological activities against cancer epithelial cells, which depend on the molecular structure of the complex, causing apoptosis, and the complex can bind to the protein drug carrier in circulation to the target tissue.
T2  - New Journal of Chemistry
T1  - Interaction, binding capacity and anticancer properties of N,N′-bis(acetylacetone)-propylenediimine-copper(II) on colorectal cancer cell line Caco-2
VL  - 45
IS  - 14
SP  - 6231
EP  - 6237
DO  - 10.1039/D1NJ00040C
ER  - 
@article{
author = "Stevanović, Nikola R. and Apostolović, Danijela and Milčić, Miloš K. and Lolić, Aleksandar and Hage, Marianne van and Ćirković-Veličković, Tanja and Baošić, Rada",
year = "2021",
abstract = "Different Schiff base complexes have biological activities that make them suitable for drug design. The biological properties of tetradentate Schiff base copper(II) complexed with N,N′-bis(acetylacetone)propylenediimine have been studied. The cytotoxic activity towards Caco-2 cells were determined by MTT, Anexin V and PI apoptosis assays. N,N′-bis(acetylacetone)propylenediimine-copper(II) showed the anti-cancer and anti-proliferative properties by inducing apoptosis in Caco-2 cells. A comparison of the cytotoxic activity of this compound with cisplatin shows that it is more effective on the colorectal cancer cell line Caco-2. The binding capacity and interaction of N,N′-bis(acetylacetone)propylenediimine-copper(II) with HSA were systemically investigated by in vitro fluorescence spectroscopy, CD spectroscopy, and in silico molecular docking study. Furthermore, in vitro and in silico interaction studies indicated that the complex binds to HSA through a static quenching mechanism without changes in protein conformation. The calculated number of binding sites was in line with molecular docking studies. The obtained Ka value suggests that the compound can be released from the protein in target cells. The tetradentate Schiff base copper(II) complex exhibited in vitro biological activities against cancer epithelial cells, which depend on the molecular structure of the complex, causing apoptosis, and the complex can bind to the protein drug carrier in circulation to the target tissue.",
journal = "New Journal of Chemistry",
title = "Interaction, binding capacity and anticancer properties of N,N′-bis(acetylacetone)-propylenediimine-copper(II) on colorectal cancer cell line Caco-2",
volume = "45",
number = "14",
pages = "6231-6237",
doi = "10.1039/D1NJ00040C"
}
Stevanović, N. R., Apostolović, D., Milčić, M. K., Lolić, A., Hage, M. v., Ćirković-Veličković, T.,& Baošić, R.. (2021). Interaction, binding capacity and anticancer properties of N,N′-bis(acetylacetone)-propylenediimine-copper(II) on colorectal cancer cell line Caco-2. in New Journal of Chemistry, 45(14), 6231-6237.
https://doi.org/10.1039/D1NJ00040C
Stevanović NR, Apostolović D, Milčić MK, Lolić A, Hage MV, Ćirković-Veličković T, Baošić R. Interaction, binding capacity and anticancer properties of N,N′-bis(acetylacetone)-propylenediimine-copper(II) on colorectal cancer cell line Caco-2. in New Journal of Chemistry. 2021;45(14):6231-6237.
doi:10.1039/D1NJ00040C .
Stevanović, Nikola R., Apostolović, Danijela, Milčić, Miloš K., Lolić, Aleksandar, Hage, Marianne van, Ćirković-Veličković, Tanja, Baošić, Rada, "Interaction, binding capacity and anticancer properties of N,N′-bis(acetylacetone)-propylenediimine-copper(II) on colorectal cancer cell line Caco-2" in New Journal of Chemistry, 45, no. 14 (2021):6231-6237,
https://doi.org/10.1039/D1NJ00040C . .

Supplementary data for the article: Stevanović, N.; Apostolović, D.; Milčić, M.; Lolić, A.; Hage, M. van; Veličković, T. Ć.; Baošić, R. Interaction, Binding Capacity and Anticancer Properties of N,N′-Bis(Acetylacetone)-Propylenediimine-Copper(II) on Colorectal Cancer Cell Line Caco-2. New J. Chem. 2021, 45 (14), 6231–6237. https://doi.org/10.1039/D1NJ00040C.

Stevanović, Nikola R.; Apostolović, Danijela; Milčić, Miloš K.; Lolić, Aleksandar; Hage, Marianne van; Ćirković-Veličković, Tanja; Baošić, Rada

(2021)

TY  - DATA
AU  - Stevanović, Nikola R.
AU  - Apostolović, Danijela
AU  - Milčić, Miloš K.
AU  - Lolić, Aleksandar
AU  - Hage, Marianne van
AU  - Ćirković-Veličković, Tanja
AU  - Baošić, Rada
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4400
T2  - New Journal of Chemistry
T1  - Supplementary data for the article: Stevanović, N.; Apostolović, D.; Milčić, M.; Lolić, A.; Hage, M. van; Veličković, T. Ć.; Baošić, R. Interaction, Binding Capacity and Anticancer Properties of N,N′-Bis(Acetylacetone)-Propylenediimine-Copper(II) on Colorectal Cancer Cell Line Caco-2. New J. Chem. 2021, 45 (14), 6231–6237. https://doi.org/10.1039/D1NJ00040C.
ER  - 
@misc{
author = "Stevanović, Nikola R. and Apostolović, Danijela and Milčić, Miloš K. and Lolić, Aleksandar and Hage, Marianne van and Ćirković-Veličković, Tanja and Baošić, Rada",
year = "2021",
journal = "New Journal of Chemistry",
title = "Supplementary data for the article: Stevanović, N.; Apostolović, D.; Milčić, M.; Lolić, A.; Hage, M. van; Veličković, T. Ć.; Baošić, R. Interaction, Binding Capacity and Anticancer Properties of N,N′-Bis(Acetylacetone)-Propylenediimine-Copper(II) on Colorectal Cancer Cell Line Caco-2. New J. Chem. 2021, 45 (14), 6231–6237. https://doi.org/10.1039/D1NJ00040C."
}
Stevanović, N. R., Apostolović, D., Milčić, M. K., Lolić, A., Hage, M. v., Ćirković-Veličković, T.,& Baošić, R.. (2021). Supplementary data for the article: Stevanović, N.; Apostolović, D.; Milčić, M.; Lolić, A.; Hage, M. van; Veličković, T. Ć.; Baošić, R. Interaction, Binding Capacity and Anticancer Properties of N,N′-Bis(Acetylacetone)-Propylenediimine-Copper(II) on Colorectal Cancer Cell Line Caco-2. New J. Chem. 2021, 45 (14), 6231–6237. https://doi.org/10.1039/D1NJ00040C.. in New Journal of Chemistry.
Stevanović NR, Apostolović D, Milčić MK, Lolić A, Hage MV, Ćirković-Veličković T, Baošić R. Supplementary data for the article: Stevanović, N.; Apostolović, D.; Milčić, M.; Lolić, A.; Hage, M. van; Veličković, T. Ć.; Baošić, R. Interaction, Binding Capacity and Anticancer Properties of N,N′-Bis(Acetylacetone)-Propylenediimine-Copper(II) on Colorectal Cancer Cell Line Caco-2. New J. Chem. 2021, 45 (14), 6231–6237. https://doi.org/10.1039/D1NJ00040C.. in New Journal of Chemistry. 2021;..
Stevanović, Nikola R., Apostolović, Danijela, Milčić, Miloš K., Lolić, Aleksandar, Hage, Marianne van, Ćirković-Veličković, Tanja, Baošić, Rada, "Supplementary data for the article: Stevanović, N.; Apostolović, D.; Milčić, M.; Lolić, A.; Hage, M. van; Veličković, T. Ć.; Baošić, R. Interaction, Binding Capacity and Anticancer Properties of N,N′-Bis(Acetylacetone)-Propylenediimine-Copper(II) on Colorectal Cancer Cell Line Caco-2. New J. Chem. 2021, 45 (14), 6231–6237. https://doi.org/10.1039/D1NJ00040C." in New Journal of Chemistry (2021).

Drying methodology effect on the phenolic content, antioxidant activity of Myrtus communis L. leaves ethanol extracts and soybean oil oxidative stability

Snoussi, Ahmed; Essaidi, Ismahen; Ben Haj Koubaier, Hayet; Zrelli, Houda; Alsafari, Ibrahim; Tešić, Živoslav Lj.; Mihailovic, Jelena; Khan, Muhummadh; El Omri, Abdelfatteh; Ćirković-Veličković, Tanja; Bouzouita, Nabiha

(Springer Nature, 2021)

TY  - JOUR
AU  - Snoussi, Ahmed
AU  - Essaidi, Ismahen
AU  - Ben Haj Koubaier, Hayet
AU  - Zrelli, Houda
AU  - Alsafari, Ibrahim
AU  - Tešić, Živoslav Lj.
AU  - Mihailovic, Jelena
AU  - Khan, Muhummadh
AU  - El Omri, Abdelfatteh
AU  - Ćirković-Veličković, Tanja
AU  - Bouzouita, Nabiha
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4441
AB  - In this study, different drying methodologies (convective air, oven and microwave) of Myrtus communis L. (M. communis L.) leaves were conducted to investigate their effects on the levels of phenolic compounds, antioxidant capacity of ethanolic extracts (EEs) as well as the soybean oil oxidative stability. Drying methodology significantly influenced the extractability of phenolic compounds. Microwave drying led to an increase in the amounts of total phenols, flavonoids and proanthocyanidins followed by oven drying at 70 °C. Higher temperature of drying (100 and 120 °C) led to a significant reduction of their amounts (p < 0.05). An ultra-performance liquid chromatography method combined with high resolution mass spectroscopic detection was used to analyze the phenolic fraction of extracts. Higher amounts of the identified compounds were observed when leaves were heat treated. Furthermore, the evaluation of the antioxidant activity showed that the studied extracts possess in general high antioxidant capacities, significantly dependent on the employed drying methodology. The incorporation of the different extracts at 200 ppm in soybean oil showed that its oxidative stability was significantly improved. Extracts from leaves treated with microwave (EE_MW) and at 70 °C (EE_70) have better effect than BHT. The results of the present study suggest that microwave drying could be useful to enhance the extractability of phenolic compounds and the antioxidant capacity of M. communis L. leaf extract.
PB  - Springer Nature
T2  - BMC Chemistry
T2  - BMC ChemistryBMC Chemistry
T1  - Drying methodology effect on the phenolic content, antioxidant activity of Myrtus communis L. leaves ethanol extracts and soybean oil oxidative stability
VL  - 15
IS  - 1
SP  - 31
DO  - 10.1186/s13065-021-00753-2
ER  - 
@article{
author = "Snoussi, Ahmed and Essaidi, Ismahen and Ben Haj Koubaier, Hayet and Zrelli, Houda and Alsafari, Ibrahim and Tešić, Živoslav Lj. and Mihailovic, Jelena and Khan, Muhummadh and El Omri, Abdelfatteh and Ćirković-Veličković, Tanja and Bouzouita, Nabiha",
year = "2021",
abstract = "In this study, different drying methodologies (convective air, oven and microwave) of Myrtus communis L. (M. communis L.) leaves were conducted to investigate their effects on the levels of phenolic compounds, antioxidant capacity of ethanolic extracts (EEs) as well as the soybean oil oxidative stability. Drying methodology significantly influenced the extractability of phenolic compounds. Microwave drying led to an increase in the amounts of total phenols, flavonoids and proanthocyanidins followed by oven drying at 70 °C. Higher temperature of drying (100 and 120 °C) led to a significant reduction of their amounts (p < 0.05). An ultra-performance liquid chromatography method combined with high resolution mass spectroscopic detection was used to analyze the phenolic fraction of extracts. Higher amounts of the identified compounds were observed when leaves were heat treated. Furthermore, the evaluation of the antioxidant activity showed that the studied extracts possess in general high antioxidant capacities, significantly dependent on the employed drying methodology. The incorporation of the different extracts at 200 ppm in soybean oil showed that its oxidative stability was significantly improved. Extracts from leaves treated with microwave (EE_MW) and at 70 °C (EE_70) have better effect than BHT. The results of the present study suggest that microwave drying could be useful to enhance the extractability of phenolic compounds and the antioxidant capacity of M. communis L. leaf extract.",
publisher = "Springer Nature",
journal = "BMC Chemistry, BMC ChemistryBMC Chemistry",
title = "Drying methodology effect on the phenolic content, antioxidant activity of Myrtus communis L. leaves ethanol extracts and soybean oil oxidative stability",
volume = "15",
number = "1",
pages = "31",
doi = "10.1186/s13065-021-00753-2"
}
Snoussi, A., Essaidi, I., Ben Haj Koubaier, H., Zrelli, H., Alsafari, I., Tešić, Ž. Lj., Mihailovic, J., Khan, M., El Omri, A., Ćirković-Veličković, T.,& Bouzouita, N.. (2021). Drying methodology effect on the phenolic content, antioxidant activity of Myrtus communis L. leaves ethanol extracts and soybean oil oxidative stability. in BMC Chemistry
Springer Nature., 15(1), 31.
https://doi.org/10.1186/s13065-021-00753-2
Snoussi A, Essaidi I, Ben Haj Koubaier H, Zrelli H, Alsafari I, Tešić ŽL, Mihailovic J, Khan M, El Omri A, Ćirković-Veličković T, Bouzouita N. Drying methodology effect on the phenolic content, antioxidant activity of Myrtus communis L. leaves ethanol extracts and soybean oil oxidative stability. in BMC Chemistry. 2021;15(1):31.
doi:10.1186/s13065-021-00753-2 .
Snoussi, Ahmed, Essaidi, Ismahen, Ben Haj Koubaier, Hayet, Zrelli, Houda, Alsafari, Ibrahim, Tešić, Živoslav Lj., Mihailovic, Jelena, Khan, Muhummadh, El Omri, Abdelfatteh, Ćirković-Veličković, Tanja, Bouzouita, Nabiha, "Drying methodology effect on the phenolic content, antioxidant activity of Myrtus communis L. leaves ethanol extracts and soybean oil oxidative stability" in BMC Chemistry, 15, no. 1 (2021):31,
https://doi.org/10.1186/s13065-021-00753-2 . .

Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome

Peruško, Marija; Apostolović, Danijela; Kiewiet, Mensiena Berentje Geertje; Grundström, Jeanette; Hamsten, Carl; Starkhammar, Maria; Ćirković-Veličković, Tanja; Hage, Marianne van

(Blackwell Publishing Ltd, 2021)

TY  - JOUR
AU  - Peruško, Marija
AU  - Apostolović, Danijela
AU  - Kiewiet, Mensiena Berentje Geertje
AU  - Grundström, Jeanette
AU  - Hamsten, Carl
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - Hage, Marianne van
PY  - 2021
UR  - https://onlinelibrary.wiley.com/doi/abs/10.1111/all.14889
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4446
AB  - Background Mammalian meat is the most common trigger of the allergic reactions in patients with α-Gal syndrome (AGS). Milk and dairy, although less often, also cause a significant number of allergic manifestations. The aim of this study was to identify α-Gal-containing bovine milk proteins with allergenic properties among AGS patients. Methods Thirty-eight AGS patients with IgE to milk were included in the study. Milk proteins were analyzed for the presence of α-Gal and for binding by patients’ IgE using immunoblot, ImmunoCAP, and inhibition ELISA. Allergenicity of milk and milk proteins was assessed by basophil activation test. Results More than half of the AGS patients reported allergic reactions to milk or dairy products. Bovine γ-globulin (BGG), lactoferrin (LF), and lactoperoxidase (LPO) were identified as α-Gal carrying proteins which were recognized by AGS patients’ IgE. Whey mirrored the anti-α-Gal and IgE reactivity of BGG, LF, and LPO. Eighty-nine percent of the patients displayed IgE to BGG, 91% to LF, and 57% to LPO. Inhibition of α-Gal-specific IgE binding was achieved by BGG, LF, LPO, and whey. These proteins also activated AGS patients’ basophils. Interestingly, at lower concentrations, LF was the most potent inhibitor of IgE binding, and the most potent activator of basophils. Conclusion BGG, LF, and LPO were all found to be relevant milk α-Gal-containing glycoproteins that bound AGS patients’ IgE antibodies and activated their basophils. These proteins are probably involved in the allergic reactions to milk in AGS patients. LPO was for the first time shown to be an allergen.
PB  - Blackwell Publishing Ltd
T2  - Allergy
T2  - Allergy
T1  - Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome
DO  - 10.1111/all.14889
ER  - 
@article{
author = "Peruško, Marija and Apostolović, Danijela and Kiewiet, Mensiena Berentje Geertje and Grundström, Jeanette and Hamsten, Carl and Starkhammar, Maria and Ćirković-Veličković, Tanja and Hage, Marianne van",
year = "2021",
abstract = "Background Mammalian meat is the most common trigger of the allergic reactions in patients with α-Gal syndrome (AGS). Milk and dairy, although less often, also cause a significant number of allergic manifestations. The aim of this study was to identify α-Gal-containing bovine milk proteins with allergenic properties among AGS patients. Methods Thirty-eight AGS patients with IgE to milk were included in the study. Milk proteins were analyzed for the presence of α-Gal and for binding by patients’ IgE using immunoblot, ImmunoCAP, and inhibition ELISA. Allergenicity of milk and milk proteins was assessed by basophil activation test. Results More than half of the AGS patients reported allergic reactions to milk or dairy products. Bovine γ-globulin (BGG), lactoferrin (LF), and lactoperoxidase (LPO) were identified as α-Gal carrying proteins which were recognized by AGS patients’ IgE. Whey mirrored the anti-α-Gal and IgE reactivity of BGG, LF, and LPO. Eighty-nine percent of the patients displayed IgE to BGG, 91% to LF, and 57% to LPO. Inhibition of α-Gal-specific IgE binding was achieved by BGG, LF, LPO, and whey. These proteins also activated AGS patients’ basophils. Interestingly, at lower concentrations, LF was the most potent inhibitor of IgE binding, and the most potent activator of basophils. Conclusion BGG, LF, and LPO were all found to be relevant milk α-Gal-containing glycoproteins that bound AGS patients’ IgE antibodies and activated their basophils. These proteins are probably involved in the allergic reactions to milk in AGS patients. LPO was for the first time shown to be an allergen.",
publisher = "Blackwell Publishing Ltd",
journal = "Allergy, Allergy",
title = "Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome",
doi = "10.1111/all.14889"
}
Peruško, M., Apostolović, D., Kiewiet, M. B. G., Grundström, J., Hamsten, C., Starkhammar, M., Ćirković-Veličković, T.,& Hage, M. v.. (2021). Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome. in Allergy
Blackwell Publishing Ltd..
https://doi.org/10.1111/all.14889
Peruško M, Apostolović D, Kiewiet MBG, Grundström J, Hamsten C, Starkhammar M, Ćirković-Veličković T, Hage MV. Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome. in Allergy. 2021;.
doi:10.1111/all.14889 .
Peruško, Marija, Apostolović, Danijela, Kiewiet, Mensiena Berentje Geertje, Grundström, Jeanette, Hamsten, Carl, Starkhammar, Maria, Ćirković-Veličković, Tanja, Hage, Marianne van, "Bovine γ-globulin, lactoferrin, and lactoperoxidase are relevant bovine milk allergens in patients with α-Gal syndrome" in Allergy (2021),
https://doi.org/10.1111/all.14889 . .
4

Supplementary data for the article: Perusko, M.; Apostolovic, D.; Kiewiet, M. B. G.; Grundström, J.; Hamsten, C.; Starkhammar, M.; Velickovic, T. C.; Hage, M. van. Bovine γ-Globulin, Lactoferrin, and Lactoperoxidase Are Relevant Bovine Milk Allergens in Patients with α-Gal Syndrome. Allergy n/a (n/a). https://doi.org/10.1111/all.14889.

Peruško, Marija; Apostolović, Danijela; Kiewiet, Mensiena Berentje Geertje; Grundström, Jeanette; Hamsten, Carl; Starkhammar, Maria; Ćirković-Veličković, Tanja; Hage, Marianne van

(Blackwell Publishing Ltd, 2021)

TY  - DATA
AU  - Peruško, Marija
AU  - Apostolović, Danijela
AU  - Kiewiet, Mensiena Berentje Geertje
AU  - Grundström, Jeanette
AU  - Hamsten, Carl
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - Hage, Marianne van
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4447
PB  - Blackwell Publishing Ltd
T2  - Allergy
T2  - Allergy
T1  - Supplementary data for the article: Perusko, M.; Apostolovic, D.; Kiewiet, M. B. G.; Grundström, J.; Hamsten, C.; Starkhammar, M.; Velickovic, T. C.; Hage, M. van. Bovine γ-Globulin, Lactoferrin, and Lactoperoxidase Are Relevant Bovine Milk Allergens in Patients with α-Gal Syndrome. Allergy n/a (n/a). https://doi.org/10.1111/all.14889.
ER  - 
@misc{
author = "Peruško, Marija and Apostolović, Danijela and Kiewiet, Mensiena Berentje Geertje and Grundström, Jeanette and Hamsten, Carl and Starkhammar, Maria and Ćirković-Veličković, Tanja and Hage, Marianne van",
year = "2021",
publisher = "Blackwell Publishing Ltd",
journal = "Allergy, Allergy",
title = "Supplementary data for the article: Perusko, M.; Apostolovic, D.; Kiewiet, M. B. G.; Grundström, J.; Hamsten, C.; Starkhammar, M.; Velickovic, T. C.; Hage, M. van. Bovine γ-Globulin, Lactoferrin, and Lactoperoxidase Are Relevant Bovine Milk Allergens in Patients with α-Gal Syndrome. Allergy n/a (n/a). https://doi.org/10.1111/all.14889."
}
Peruško, M., Apostolović, D., Kiewiet, M. B. G., Grundström, J., Hamsten, C., Starkhammar, M., Ćirković-Veličković, T.,& Hage, M. v.. (2021). Supplementary data for the article: Perusko, M.; Apostolovic, D.; Kiewiet, M. B. G.; Grundström, J.; Hamsten, C.; Starkhammar, M.; Velickovic, T. C.; Hage, M. van. Bovine γ-Globulin, Lactoferrin, and Lactoperoxidase Are Relevant Bovine Milk Allergens in Patients with α-Gal Syndrome. Allergy n/a (n/a). https://doi.org/10.1111/all.14889.. in Allergy
Blackwell Publishing Ltd..
Peruško M, Apostolović D, Kiewiet MBG, Grundström J, Hamsten C, Starkhammar M, Ćirković-Veličković T, Hage MV. Supplementary data for the article: Perusko, M.; Apostolovic, D.; Kiewiet, M. B. G.; Grundström, J.; Hamsten, C.; Starkhammar, M.; Velickovic, T. C.; Hage, M. van. Bovine γ-Globulin, Lactoferrin, and Lactoperoxidase Are Relevant Bovine Milk Allergens in Patients with α-Gal Syndrome. Allergy n/a (n/a). https://doi.org/10.1111/all.14889.. in Allergy. 2021;..
Peruško, Marija, Apostolović, Danijela, Kiewiet, Mensiena Berentje Geertje, Grundström, Jeanette, Hamsten, Carl, Starkhammar, Maria, Ćirković-Veličković, Tanja, Hage, Marianne van, "Supplementary data for the article: Perusko, M.; Apostolovic, D.; Kiewiet, M. B. G.; Grundström, J.; Hamsten, C.; Starkhammar, M.; Velickovic, T. C.; Hage, M. van. Bovine γ-Globulin, Lactoferrin, and Lactoperoxidase Are Relevant Bovine Milk Allergens in Patients with α-Gal Syndrome. Allergy n/a (n/a). https://doi.org/10.1111/all.14889." in Allergy (2021).

Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application

Đurđić, Slađana Z.; Stanković, V.; Vlahović, Filip; Ognjanović, Miloš; Kalcher, K.; Ćirković-Veličković, Tanja; Mutić, Jelena; Stanković, Dalibor

(The Electrochemical Society (ECS), 2021)

TY  - JOUR
AU  - Đurđić, Slađana Z.
AU  - Stanković, V.
AU  - Vlahović, Filip
AU  - Ognjanović, Miloš
AU  - Kalcher, K.
AU  - Ćirković-Veličković, Tanja
AU  - Mutić, Jelena
AU  - Stanković, Dalibor
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4474
AB  - Based on graphene nanoplatelets capability to build block composites, as well as well-known electrochemical characteristic of the manganese oxide materials, in the present research, a nanocomposite, formed from graphene nanoplatelets (GNP) and manganese(IV)-oxide (MnO2) nanoparticles, has been proposed as a novel and convenient support for enzyme immobilization. Performance of screen printed carbon electrodes (SPCEs) was significantly improved after their modification with GNP@MnO2 (SPCE/GNP@MnO2). The polyphenolic index biosensor was prepared by applying the drop coating technique using laccase and Nafion®. Developed biosensor shows a fast and reliable amperometric response toward caffeic acid, as a model compound, at operating potential of +0.40 V (vs Ag/AgCl), with a wide linear range and detection limit of 1.9 μmol l−1. Developed procedure was successfully applied for the determination of polyphenolic indexes in wine samples. Recovery tests indicate excellent accuracy and precision of the method, concluding that the biosensor can offer a fast, accurate, reliable and precise determination of the polyphenolic index. More importantly, our results suggest a great potential for the application in real samples.
PB  - The Electrochemical Society (ECS)
T2  - Journal of The Electrochemical Society
T1  - Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application
VL  - 168
IS  - 3
SP  - 037510
DO  - 10.1149/1945-7111/abeaf2
ER  - 
@article{
author = "Đurđić, Slađana Z. and Stanković, V. and Vlahović, Filip and Ognjanović, Miloš and Kalcher, K. and Ćirković-Veličković, Tanja and Mutić, Jelena and Stanković, Dalibor",
year = "2021",
abstract = "Based on graphene nanoplatelets capability to build block composites, as well as well-known electrochemical characteristic of the manganese oxide materials, in the present research, a nanocomposite, formed from graphene nanoplatelets (GNP) and manganese(IV)-oxide (MnO2) nanoparticles, has been proposed as a novel and convenient support for enzyme immobilization. Performance of screen printed carbon electrodes (SPCEs) was significantly improved after their modification with GNP@MnO2 (SPCE/GNP@MnO2). The polyphenolic index biosensor was prepared by applying the drop coating technique using laccase and Nafion®. Developed biosensor shows a fast and reliable amperometric response toward caffeic acid, as a model compound, at operating potential of +0.40 V (vs Ag/AgCl), with a wide linear range and detection limit of 1.9 μmol l−1. Developed procedure was successfully applied for the determination of polyphenolic indexes in wine samples. Recovery tests indicate excellent accuracy and precision of the method, concluding that the biosensor can offer a fast, accurate, reliable and precise determination of the polyphenolic index. More importantly, our results suggest a great potential for the application in real samples.",
publisher = "The Electrochemical Society (ECS)",
journal = "Journal of The Electrochemical Society",
title = "Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application",
volume = "168",
number = "3",
pages = "037510",
doi = "10.1149/1945-7111/abeaf2"
}
Đurđić, S. Z., Stanković, V., Vlahović, F., Ognjanović, M., Kalcher, K., Ćirković-Veličković, T., Mutić, J.,& Stanković, D.. (2021). Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application. in Journal of The Electrochemical Society
The Electrochemical Society (ECS)., 168(3), 037510.
https://doi.org/10.1149/1945-7111/abeaf2
Đurđić SZ, Stanković V, Vlahović F, Ognjanović M, Kalcher K, Ćirković-Veličković T, Mutić J, Stanković D. Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application. in Journal of The Electrochemical Society. 2021;168(3):037510.
doi:10.1149/1945-7111/abeaf2 .
Đurđić, Slađana Z., Stanković, V., Vlahović, Filip, Ognjanović, Miloš, Kalcher, K., Ćirković-Veličković, Tanja, Mutić, Jelena, Stanković, Dalibor, "Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application" in Journal of The Electrochemical Society, 168, no. 3 (2021):037510,
https://doi.org/10.1149/1945-7111/abeaf2 . .
1

Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application

Đurđić, Slađana Z.; Stanković, V.; Vlahović, Filip; Ognjanović, Miloš; Kalcher, K.; Ćirković-Veličković, Tanja; Mutić, Jelena; Stanković, Dalibor

(The Electrochemical Society (ECS), 2021)

TY  - JOUR
AU  - Đurđić, Slađana Z.
AU  - Stanković, V.
AU  - Vlahović, Filip
AU  - Ognjanović, Miloš
AU  - Kalcher, K.
AU  - Ćirković-Veličković, Tanja
AU  - Mutić, Jelena
AU  - Stanković, Dalibor
PY  - 2021
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4475
AB  - Based on graphene nanoplatelets capability to build block composites, as well as well-known electrochemical characteristic of the manganese oxide materials, in the present research, a nanocomposite, formed from graphene nanoplatelets (GNP) and manganese(IV)-oxide (MnO2) nanoparticles, has been proposed as a novel and convenient support for enzyme immobilization. Performance of screen printed carbon electrodes (SPCEs) was significantly improved after their modification with GNP@MnO2 (SPCE/GNP@MnO2). The polyphenolic index biosensor was prepared by applying the drop coating technique using laccase and Nafion®. Developed biosensor shows a fast and reliable amperometric response toward caffeic acid, as a model compound, at operating potential of +0.40 V (vs Ag/AgCl), with a wide linear range and detection limit of 1.9 μmol l−1. Developed procedure was successfully applied for the determination of polyphenolic indexes in wine samples. Recovery tests indicate excellent accuracy and precision of the method, concluding that the biosensor can offer a fast, accurate, reliable and precise determination of the polyphenolic index. More importantly, our results suggest a great potential for the application in real samples.
PB  - The Electrochemical Society (ECS)
T2  - Journal of The Electrochemical Society
T1  - Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application
VL  - 168
IS  - 3
SP  - 037510
DO  - 10.1149/1945-7111/abeaf2
ER  - 
@article{
author = "Đurđić, Slađana Z. and Stanković, V. and Vlahović, Filip and Ognjanović, Miloš and Kalcher, K. and Ćirković-Veličković, Tanja and Mutić, Jelena and Stanković, Dalibor",
year = "2021",
abstract = "Based on graphene nanoplatelets capability to build block composites, as well as well-known electrochemical characteristic of the manganese oxide materials, in the present research, a nanocomposite, formed from graphene nanoplatelets (GNP) and manganese(IV)-oxide (MnO2) nanoparticles, has been proposed as a novel and convenient support for enzyme immobilization. Performance of screen printed carbon electrodes (SPCEs) was significantly improved after their modification with GNP@MnO2 (SPCE/GNP@MnO2). The polyphenolic index biosensor was prepared by applying the drop coating technique using laccase and Nafion®. Developed biosensor shows a fast and reliable amperometric response toward caffeic acid, as a model compound, at operating potential of +0.40 V (vs Ag/AgCl), with a wide linear range and detection limit of 1.9 μmol l−1. Developed procedure was successfully applied for the determination of polyphenolic indexes in wine samples. Recovery tests indicate excellent accuracy and precision of the method, concluding that the biosensor can offer a fast, accurate, reliable and precise determination of the polyphenolic index. More importantly, our results suggest a great potential for the application in real samples.",
publisher = "The Electrochemical Society (ECS)",
journal = "Journal of The Electrochemical Society",
title = "Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application",
volume = "168",
number = "3",
pages = "037510",
doi = "10.1149/1945-7111/abeaf2"
}
Đurđić, S. Z., Stanković, V., Vlahović, F., Ognjanović, M., Kalcher, K., Ćirković-Veličković, T., Mutić, J.,& Stanković, D.. (2021). Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application. in Journal of The Electrochemical Society
The Electrochemical Society (ECS)., 168(3), 037510.
https://doi.org/10.1149/1945-7111/abeaf2
Đurđić SZ, Stanković V, Vlahović F, Ognjanović M, Kalcher K, Ćirković-Veličković T, Mutić J, Stanković D. Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application. in Journal of The Electrochemical Society. 2021;168(3):037510.
doi:10.1149/1945-7111/abeaf2 .
Đurđić, Slađana Z., Stanković, V., Vlahović, Filip, Ognjanović, Miloš, Kalcher, K., Ćirković-Veličković, Tanja, Mutić, Jelena, Stanković, Dalibor, "Laccase Polyphenolic Biosensor Supported on MnO2@GNP Decorated SPCE: Preparation, Characterization, and Analytical Application" in Journal of The Electrochemical Society, 168, no. 3 (2021):037510,
https://doi.org/10.1149/1945-7111/abeaf2 . .
1

Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation

Gligorijević, Nikola; Radomirović, Mirjana Ž.; Rajković, Andreja; Nedić, Olgica; Ćirković-Veličković, Tanja

(Multidisciplinary Digital Publishing Institute (MDPI), 2020)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Radomirović, Mirjana Ž.
AU  - Rajković, Andreja
AU  - Nedić, Olgica
AU  - Ćirković-Veličković, Tanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4235
AB  - The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, as it was later discovered that the presence of antioxidants, including resveratrol, have beneficial effects. We hypothesized that resveratrol may have a more direct role in protection from harmful oxidation, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetry demonstrated that resveratrol is capable of binding to fibrinogen, the main protein in the coagulation process, which is also important as a food additive. Various spectroscopic methods determined that binding does not cause fibrinogen unfolding or destabilization since protein melting temperature remains unchanged. A mutually protective effect against the free radical-induced oxidation of polyphenol and fibrinogen was found. The presence of fibrinogen caused only a negligible masking effect of the antioxidative abilities of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing its potential bioavailability. Due to its interaction with fibrinogen, resveratrol may serve as an antioxidant at the site of injury. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.
PB  - Multidisciplinary Digital Publishing Institute (MDPI)
T2  - Foods
T1  - Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation
VL  - 9
IS  - 6
SP  - 780
DO  - 10.3390/foods9060780
ER  - 
@article{
author = "Gligorijević, Nikola and Radomirović, Mirjana Ž. and Rajković, Andreja and Nedić, Olgica and Ćirković-Veličković, Tanja",
year = "2020",
abstract = "The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, as it was later discovered that the presence of antioxidants, including resveratrol, have beneficial effects. We hypothesized that resveratrol may have a more direct role in protection from harmful oxidation, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetry demonstrated that resveratrol is capable of binding to fibrinogen, the main protein in the coagulation process, which is also important as a food additive. Various spectroscopic methods determined that binding does not cause fibrinogen unfolding or destabilization since protein melting temperature remains unchanged. A mutually protective effect against the free radical-induced oxidation of polyphenol and fibrinogen was found. The presence of fibrinogen caused only a negligible masking effect of the antioxidative abilities of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing its potential bioavailability. Due to its interaction with fibrinogen, resveratrol may serve as an antioxidant at the site of injury. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
journal = "Foods",
title = "Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation",
volume = "9",
number = "6",
pages = "780",
doi = "10.3390/foods9060780"
}
Gligorijević, N., Radomirović, M. Ž., Rajković, A., Nedić, O.,& Ćirković-Veličković, T.. (2020). Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation. in Foods
Multidisciplinary Digital Publishing Institute (MDPI)., 9(6), 780.
https://doi.org/10.3390/foods9060780
Gligorijević N, Radomirović MŽ, Rajković A, Nedić O, Ćirković-Veličković T. Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation. in Foods. 2020;9(6):780.
doi:10.3390/foods9060780 .
Gligorijević, Nikola, Radomirović, Mirjana Ž., Rajković, Andreja, Nedić, Olgica, Ćirković-Veličković, Tanja, "Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation" in Foods, 9, no. 6 (2020):780,
https://doi.org/10.3390/foods9060780 . .
2
2
1

Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy

Apostolović, Danijela; Mihailović, Jelena; Commins, Scott P.; Wijnveld, Michiel; Kazimirova, Maria; Starkhammar, Maria; Stockinger, Hannes; Platts-Mills, Thomas A. E.; Ćirković-Veličković, Tanja; Hamsten, Carl; van Hage, Marianne

(Wiley, 2020)

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Commins, Scott P.
AU  - Wijnveld, Michiel
AU  - Kazimirova, Maria
AU  - Starkhammar, Maria
AU  - Stockinger, Hannes
AU  - Platts-Mills, Thomas A. E.
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3860
PB  - Wiley
T2  - Allergy: European Journal of Allergy and Clinical Immunology
T1  - Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy
VL  - 75
IS  - 1
SP  - 217
EP  - 220
DO  - 10.1111/ALL.13978
ER  - 
@article{
author = "Apostolović, Danijela and Mihailović, Jelena and Commins, Scott P. and Wijnveld, Michiel and Kazimirova, Maria and Starkhammar, Maria and Stockinger, Hannes and Platts-Mills, Thomas A. E. and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2020",
publisher = "Wiley",
journal = "Allergy: European Journal of Allergy and Clinical Immunology",
title = "Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy",
volume = "75",
number = "1",
pages = "217-220",
doi = "10.1111/ALL.13978"
}
Apostolović, D., Mihailović, J., Commins, S. P., Wijnveld, M., Kazimirova, M., Starkhammar, M., Stockinger, H., Platts-Mills, T. A. E., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M.. (2020). Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy. in Allergy: European Journal of Allergy and Clinical Immunology
Wiley., 75(1), 217-220.
https://doi.org/10.1111/ALL.13978
Apostolović D, Mihailović J, Commins SP, Wijnveld M, Kazimirova M, Starkhammar M, Stockinger H, Platts-Mills TAE, Ćirković-Veličković T, Hamsten C, van Hage M. Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy. in Allergy: European Journal of Allergy and Clinical Immunology. 2020;75(1):217-220.
doi:10.1111/ALL.13978 .
Apostolović, Danijela, Mihailović, Jelena, Commins, Scott P., Wijnveld, Michiel, Kazimirova, Maria, Starkhammar, Maria, Stockinger, Hannes, Platts-Mills, Thomas A. E., Ćirković-Veličković, Tanja, Hamsten, Carl, van Hage, Marianne, "Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy" in Allergy: European Journal of Allergy and Clinical Immunology, 75, no. 1 (2020):217-220,
https://doi.org/10.1111/ALL.13978 . .
10
21
20
20

Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy

Apostolović, Danijela; Mihailović, Jelena; Commins, Scott P.; Wijnveld, Michiel; Kazimirova, Maria; Starkhammar, Maria; Stockinger, Hannes; Platts-Mills, Thomas A. E.; Ćirković-Veličković, Tanja; Hamsten, Carl; van Hage, Marianne

(Wiley, 2020)

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Commins, Scott P.
AU  - Wijnveld, Michiel
AU  - Kazimirova, Maria
AU  - Starkhammar, Maria
AU  - Stockinger, Hannes
AU  - Platts-Mills, Thomas A. E.
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3853
PB  - Wiley
T2  - Allergy: European Journal of Allergy and Clinical Immunology
T1  - Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy
VL  - 75
IS  - 1
SP  - 217
EP  - 220
DO  - 10.1111/all.13978
ER  - 
@article{
author = "Apostolović, Danijela and Mihailović, Jelena and Commins, Scott P. and Wijnveld, Michiel and Kazimirova, Maria and Starkhammar, Maria and Stockinger, Hannes and Platts-Mills, Thomas A. E. and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2020",
publisher = "Wiley",
journal = "Allergy: European Journal of Allergy and Clinical Immunology",
title = "Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy",
volume = "75",
number = "1",
pages = "217-220",
doi = "10.1111/all.13978"
}
Apostolović, D., Mihailović, J., Commins, S. P., Wijnveld, M., Kazimirova, M., Starkhammar, M., Stockinger, H., Platts-Mills, T. A. E., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M.. (2020). Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy. in Allergy: European Journal of Allergy and Clinical Immunology
Wiley., 75(1), 217-220.
https://doi.org/10.1111/all.13978
Apostolović D, Mihailović J, Commins SP, Wijnveld M, Kazimirova M, Starkhammar M, Stockinger H, Platts-Mills TAE, Ćirković-Veličković T, Hamsten C, van Hage M. Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy. in Allergy: European Journal of Allergy and Clinical Immunology. 2020;75(1):217-220.
doi:10.1111/all.13978 .
Apostolović, Danijela, Mihailović, Jelena, Commins, Scott P., Wijnveld, Michiel, Kazimirova, Maria, Starkhammar, Maria, Stockinger, Hannes, Platts-Mills, Thomas A. E., Ćirković-Veličković, Tanja, Hamsten, Carl, van Hage, Marianne, "Allergenomics of the tick Ixodes ricinus reveal important α-Gal-carrying IgE-binding proteins in red meat allergy" in Allergy: European Journal of Allergy and Clinical Immunology, 75, no. 1 (2020):217-220,
https://doi.org/10.1111/all.13978 . .
10
21
20
20

The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c

Stanić-Vučinić, Dragana; Nikolić, Stefan; Vlajić, Katarina; Radomirović, Mirjana Ž.; Mihailović, Jelena; Ćirković-Veličković, Tanja; Grgurić-Šipka, Sanja

(Springer, 2020)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Vlajić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić-Šipka, Sanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3859
AB  - The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.
PB  - Springer
T2  - Journal of Biological Inorganic Chemistry
T1  - The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c
VL  - 25
IS  - 2
SP  - 253
EP  - 265
DO  - 10.1007/s00775-020-01758-3
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Nikolić, Stefan and Vlajić, Katarina and Radomirović, Mirjana Ž. and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić-Šipka, Sanja",
year = "2020",
abstract = "The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.",
publisher = "Springer",
journal = "Journal of Biological Inorganic Chemistry",
title = "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c",
volume = "25",
number = "2",
pages = "253-265",
doi = "10.1007/s00775-020-01758-3"
}
Stanić-Vučinić, D., Nikolić, S., Vlajić, K., Radomirović, M. Ž., Mihailović, J., Ćirković-Veličković, T.,& Grgurić-Šipka, S.. (2020). The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. in Journal of Biological Inorganic Chemistry
Springer., 25(2), 253-265.
https://doi.org/10.1007/s00775-020-01758-3
Stanić-Vučinić D, Nikolić S, Vlajić K, Radomirović MŽ, Mihailović J, Ćirković-Veličković T, Grgurić-Šipka S. The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. in Journal of Biological Inorganic Chemistry. 2020;25(2):253-265.
doi:10.1007/s00775-020-01758-3 .
Stanić-Vučinić, Dragana, Nikolić, Stefan, Vlajić, Katarina, Radomirović, Mirjana Ž., Mihailović, Jelena, Ćirković-Veličković, Tanja, Grgurić-Šipka, Sanja, "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c" in Journal of Biological Inorganic Chemistry, 25, no. 2 (2020):253-265,
https://doi.org/10.1007/s00775-020-01758-3 . .
3
3
1

Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3

Stanić-Vučinić, Dragana; Nikolić, Stefan; Vlajić, Katarina; Radomirović, Mirjana Ž.; Mihailović, Jelena; Ćirković-Veličković, Tanja; Grgurić-Šipka, Sanja

(Springer, 2020)

TY  - DATA
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Vlajić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić-Šipka, Sanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3863
PB  - Springer
T2  - Journal of Biological Inorganic Chemistry
T1  - Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3
ER  - 
@misc{
author = "Stanić-Vučinić, Dragana and Nikolić, Stefan and Vlajić, Katarina and Radomirović, Mirjana Ž. and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić-Šipka, Sanja",
year = "2020",
publisher = "Springer",
journal = "Journal of Biological Inorganic Chemistry",
title = "Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3"
}
Stanić-Vučinić, D., Nikolić, S., Vlajić, K., Radomirović, M. Ž., Mihailović, J., Ćirković-Veličković, T.,& Grgurić-Šipka, S.. (2020). Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3. in Journal of Biological Inorganic Chemistry
Springer..
Stanić-Vučinić D, Nikolić S, Vlajić K, Radomirović MŽ, Mihailović J, Ćirković-Veličković T, Grgurić-Šipka S. Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3. in Journal of Biological Inorganic Chemistry. 2020;..
Stanić-Vučinić, Dragana, Nikolić, Stefan, Vlajić, Katarina, Radomirović, Mirjana Ž., Mihailović, Jelena, Ćirković-Veličković, Tanja, Grgurić-Šipka, Sanja, "Supplementary data for the article: Stanic-Vucinic, D.; Nikolic, S.; Vlajic, K.; Radomirovic, M.; Mihailovic, J.; Cirkovic Velickovic, T.; Grguric-Sipka, S. The Interactions of the Ruthenium(II)-Cymene Complexes with Lysozyme and Cytochrome c. Journal of Biological Inorganic Chemistry 2020. https://doi.org/10.1007/s00775-020-01758-3" in Journal of Biological Inorganic Chemistry (2020).

Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978

Apostolović, Danijela; Mihailović, Jelena; Commins, Scott P.; Wijnveld, Michiel; Kazimirova, Maria; Starkhammar, Maria; Stockinger, Hannes; Platts-Mills, Thomas A. E.; Ćirković-Veličković, Tanja; Hamsten, Carl; van Hage, Marianne

(Wiley, 2020)

TY  - DATA
AU  - Apostolović, Danijela
AU  - Mihailović, Jelena
AU  - Commins, Scott P.
AU  - Wijnveld, Michiel
AU  - Kazimirova, Maria
AU  - Starkhammar, Maria
AU  - Stockinger, Hannes
AU  - Platts-Mills, Thomas A. E.
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3864
PB  - Wiley
T2  - Allergy: European Journal of Allergy and Clinical Immunology
T1  - Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978
ER  - 
@misc{
author = "Apostolović, Danijela and Mihailović, Jelena and Commins, Scott P. and Wijnveld, Michiel and Kazimirova, Maria and Starkhammar, Maria and Stockinger, Hannes and Platts-Mills, Thomas A. E. and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2020",
publisher = "Wiley",
journal = "Allergy: European Journal of Allergy and Clinical Immunology",
title = "Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978"
}
Apostolović, D., Mihailović, J., Commins, S. P., Wijnveld, M., Kazimirova, M., Starkhammar, M., Stockinger, H., Platts-Mills, T. A. E., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M.. (2020). Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978. in Allergy: European Journal of Allergy and Clinical Immunology
Wiley..
Apostolović D, Mihailović J, Commins SP, Wijnveld M, Kazimirova M, Starkhammar M, Stockinger H, Platts-Mills TAE, Ćirković-Veličković T, Hamsten C, van Hage M. Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978. in Allergy: European Journal of Allergy and Clinical Immunology. 2020;..
Apostolović, Danijela, Mihailović, Jelena, Commins, Scott P., Wijnveld, Michiel, Kazimirova, Maria, Starkhammar, Maria, Stockinger, Hannes, Platts-Mills, Thomas A. E., Ćirković-Veličković, Tanja, Hamsten, Carl, van Hage, Marianne, "Supplementary data for the article: Apostolovic, D.; Mihailovic, J.; Commins, S. P.; Wijnveld, M.; Kazimirova, M.; Starkhammar, M.; Stockinger, H.; Platts-Mills, T. A. E.; Cirkovic Velickovic, T.; Hamsten, C.; et al. Allergenomics of the Tick Ixodes Ricinus Reveals Important α-Gal–Carrying IgE-Binding Proteins in Red Meat Allergy. Allergy: European Journal of Allergy and Clinical Immunology 2020, 75 (1), 217–220. https://doi.org/10.1111/all.13978" in Allergy: European Journal of Allergy and Clinical Immunology (2020).

Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis

Moons, Jens; de Azambuja, Francisco; Mihailović, Jelena; Kozma, Karoly; Smiljanić, Katarina; Amiri, Mehran; Ćirković-Veličković, Tanja; Nyman, May; Parac-Vogt, Tatjana

(Wiley, 2020)

TY  - JOUR
AU  - Moons, Jens
AU  - de Azambuja, Francisco
AU  - Mihailović, Jelena
AU  - Kozma, Karoly
AU  - Smiljanić, Katarina
AU  - Amiri, Mehran
AU  - Ćirković-Veličković, Tanja
AU  - Nyman, May
AU  - Parac-Vogt, Tatjana
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3917
AB  - The selective hydrolysis of proteins by non‐enzymatic catalysis is difficult to achieve, yet it is crucial for applications in biotechnology and proteomics. Herein, we report that discrete hafnium metal‐oxo cluster [Hf18O10(OH)26(SO4)13⋅(H2O)33] (Hf18), which is centred by the same hexamer motif found in many MOFs, acts as a heterogeneous catalyst for the efficient hydrolysis of horse heart myoglobin (HHM) in low buffer concentrations. Among 154 amino acids present in the sequence of HHM, strictly selective cleavage at only 6 solvent accessible aspartate residues was observed. Mechanistic experiments suggest that the hydrolytic activity is likely derived from the actuation of HfIV Lewis acidic sites and the Brønsted acidic surface of Hf18. X‐ray scattering and ESI‐MS revealed that Hf18 is completely insoluble in these conditions, confirming the HHM hydrolysis is caused by a heterogeneous reaction of the solid Hf18 cluster, and not from smaller, soluble Hf species that could leach into solution.
PB  - Wiley
T2  - Angewandte Chemie (International Edition)
T1  - Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis
VL  - 59
IS  - 17
SP  - 1
EP  - 9
DO  - 10.1002/anie.202001036
ER  - 
@article{
author = "Moons, Jens and de Azambuja, Francisco and Mihailović, Jelena and Kozma, Karoly and Smiljanić, Katarina and Amiri, Mehran and Ćirković-Veličković, Tanja and Nyman, May and Parac-Vogt, Tatjana",
year = "2020",
abstract = "The selective hydrolysis of proteins by non‐enzymatic catalysis is difficult to achieve, yet it is crucial for applications in biotechnology and proteomics. Herein, we report that discrete hafnium metal‐oxo cluster [Hf18O10(OH)26(SO4)13⋅(H2O)33] (Hf18), which is centred by the same hexamer motif found in many MOFs, acts as a heterogeneous catalyst for the efficient hydrolysis of horse heart myoglobin (HHM) in low buffer concentrations. Among 154 amino acids present in the sequence of HHM, strictly selective cleavage at only 6 solvent accessible aspartate residues was observed. Mechanistic experiments suggest that the hydrolytic activity is likely derived from the actuation of HfIV Lewis acidic sites and the Brønsted acidic surface of Hf18. X‐ray scattering and ESI‐MS revealed that Hf18 is completely insoluble in these conditions, confirming the HHM hydrolysis is caused by a heterogeneous reaction of the solid Hf18 cluster, and not from smaller, soluble Hf species that could leach into solution.",
publisher = "Wiley",
journal = "Angewandte Chemie (International Edition)",
title = "Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis",
volume = "59",
number = "17",
pages = "1-9",
doi = "10.1002/anie.202001036"
}
Moons, J., de Azambuja, F., Mihailović, J., Kozma, K., Smiljanić, K., Amiri, M., Ćirković-Veličković, T., Nyman, M.,& Parac-Vogt, T.. (2020). Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis. in Angewandte Chemie (International Edition)
Wiley., 59(17), 1-9.
https://doi.org/10.1002/anie.202001036
Moons J, de Azambuja F, Mihailović J, Kozma K, Smiljanić K, Amiri M, Ćirković-Veličković T, Nyman M, Parac-Vogt T. Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis. in Angewandte Chemie (International Edition). 2020;59(17):1-9.
doi:10.1002/anie.202001036 .
Moons, Jens, de Azambuja, Francisco, Mihailović, Jelena, Kozma, Karoly, Smiljanić, Katarina, Amiri, Mehran, Ćirković-Veličković, Tanja, Nyman, May, Parac-Vogt, Tatjana, "Discrete Hf18 Metal‐oxo Cluster as a Heterogeneous Nanozyme for Site‐Specific Proteolysis" in Angewandte Chemie (International Edition), 59, no. 17 (2020):1-9,
https://doi.org/10.1002/anie.202001036 . .
22
11
10
12

The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c

Stanić-Vučinić, Dragana; Nikolić, Stefan; Vlajić, Katarina; Radomirović, Mirjana Ž.; Mihailović, Jelena; Ćirković-Veličković, Tanja; Grgurić-Šipka, Sanja

(Springer, 2020)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Stefan
AU  - Vlajić, Katarina
AU  - Radomirović, Mirjana Ž.
AU  - Mihailović, Jelena
AU  - Ćirković-Veličković, Tanja
AU  - Grgurić-Šipka, Sanja
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3942
AB  - The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.
PB  - Springer
T2  - Journal of Biological Inorganic Chemistry
T1  - The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c
VL  - 25
IS  - 2
SP  - 253
EP  - 265
DO  - 10.1007/s00775-020-01758-3
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Nikolić, Stefan and Vlajić, Katarina and Radomirović, Mirjana Ž. and Mihailović, Jelena and Ćirković-Veličković, Tanja and Grgurić-Šipka, Sanja",
year = "2020",
abstract = "The reactions of four cymene-capped ruthenium(II) compounds with pro-apaptotic protein, cytochrome c (Cyt), and anti-proliferating protein lysozyme (Ly) in carbonate buffer were investigated by ESI-MS, UV–Vis absorption and CD spectroscopy. The complexes with two chloride ligands (C2 and C3) were more reactive toward proteins than those with only one (C1 and C4), and the complex with S,N-chelating ligand (C4) was less reactive than one with O,N-chelating ligand (C1). Dehalogenated complexes are most likely species initially coordinating proteins for all tested complexes. During the time, protein adducts vividly exchanged non-arene organic ligand L with CO32- and OH-, while cymene moiety was retained. In water, only dehalogenated adducts were identified suggesting that in vivo, in the presence of various anions, dynamic ligand exchange could generate different intermediate protein species. Although all complexes reduced Cyt, the reduction was not dependent on their reactivity to protein, implying that initially noncovalent binding to Cyt occures, causing its reduction, followed by coordination to protein. Cyt reduction was accompanied with rupture of ferro-Met 80 and occupation of this hem coordination site by a histidine His-33/26. Therefore, in Cyt with C2 and C3 less intensive reduction of hem iron leave more unoccupied target residues for Ru coordination, leading to more efficient formation of covalent adducts, in comparison to C1 and C4. This study contribute to development of new protein-targeted Ru(II) cymene complexes, and to design of new cancer therapies based on targeted delivery of Ru(II) arene complexes bound on pro-apoptotic/anti-proliferating proteins as vehicles.",
publisher = "Springer",
journal = "Journal of Biological Inorganic Chemistry",
title = "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c",
volume = "25",
number = "2",
pages = "253-265",
doi = "10.1007/s00775-020-01758-3"
}
Stanić-Vučinić, D., Nikolić, S., Vlajić, K., Radomirović, M. Ž., Mihailović, J., Ćirković-Veličković, T.,& Grgurić-Šipka, S.. (2020). The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. in Journal of Biological Inorganic Chemistry
Springer., 25(2), 253-265.
https://doi.org/10.1007/s00775-020-01758-3
Stanić-Vučinić D, Nikolić S, Vlajić K, Radomirović MŽ, Mihailović J, Ćirković-Veličković T, Grgurić-Šipka S. The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c. in Journal of Biological Inorganic Chemistry. 2020;25(2):253-265.
doi:10.1007/s00775-020-01758-3 .
Stanić-Vučinić, Dragana, Nikolić, Stefan, Vlajić, Katarina, Radomirović, Mirjana Ž., Mihailović, Jelena, Ćirković-Veličković, Tanja, Grgurić-Šipka, Sanja, "The interactions of the ruthenium(II)-cymene complexes with lysozyme and cytochrome c" in Journal of Biological Inorganic Chemistry, 25, no. 2 (2020):253-265,
https://doi.org/10.1007/s00775-020-01758-3 . .
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1

Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin

Zhang, Tingting; Hu, Zongyi; Cheng, Yongwei; Xu, Haoxie; Ćirković-Veličković, Tanja; He, Kan; Sun, Fan; He, Zhendan; Liu, Zhigang; Wu, Xuli

(American Chemical Society, 2020)

TY  - JOUR
AU  - Zhang, Tingting
AU  - Hu, Zongyi
AU  - Cheng, Yongwei
AU  - Xu, Haoxie
AU  - Ćirković-Veličković, Tanja
AU  - He, Kan
AU  - Sun, Fan
AU  - He, Zhendan
AU  - Liu, Zhigang
AU  - Wu, Xuli
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3953
AB  - A previous study demonstrated decreased allergenicity in vitro of some food allergens after conjugation with polyphenols. However, little is known about how polyphenol conjugation with food allergens affects in vivo allergenicity. We conjugated a well-known food allergen, ovalbumin (OVA), with quercetin (QUE) to assess the potential allergenicity of OVA in vitro and in vivo in a BALB/c mouse model. QUE could covalently conjugate with OVA and changed the protein structure, which might destroy and/or mask OVA epitopes. Conjugation with QUE decreased IgE binding properties and the release capacity of the conjugated OVA. In vivo, as compared with native protein, conjugation with QUE decreased the levels of IgE, IgG1, IgG, plasma histamine, and mast cell protease-1 (mMCP-1) on the surface of sensitized mast cells, along with decreased FcϵRI+ and c-kit+ expression. The levels of Th2-related cytokines (IL-4, IL-5, IL-13) decreased and that of a Th1-related cytokine (IFN-Î) increased slightly, which suggests that conjugation with QUE modulated the imbalance of the Th1/Th2 immune response. Conjugation of OVA with QUE could reduce OVA allergenicity in vitro and in vivo, which could provide information for reducing food allergenicity by conjugation with polyphenols. Copyright © 2020 American Chemical Society.
PB  - American Chemical Society
T2  - Journal of Agricultural and Food Chemistry
T1  - Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin
VL  - 68
IS  - 13
SP  - 4027
EP  - 4035
DO  - 10.1021/acs.jafc.0c00461
ER  - 
@article{
author = "Zhang, Tingting and Hu, Zongyi and Cheng, Yongwei and Xu, Haoxie and Ćirković-Veličković, Tanja and He, Kan and Sun, Fan and He, Zhendan and Liu, Zhigang and Wu, Xuli",
year = "2020",
abstract = "A previous study demonstrated decreased allergenicity in vitro of some food allergens after conjugation with polyphenols. However, little is known about how polyphenol conjugation with food allergens affects in vivo allergenicity. We conjugated a well-known food allergen, ovalbumin (OVA), with quercetin (QUE) to assess the potential allergenicity of OVA in vitro and in vivo in a BALB/c mouse model. QUE could covalently conjugate with OVA and changed the protein structure, which might destroy and/or mask OVA epitopes. Conjugation with QUE decreased IgE binding properties and the release capacity of the conjugated OVA. In vivo, as compared with native protein, conjugation with QUE decreased the levels of IgE, IgG1, IgG, plasma histamine, and mast cell protease-1 (mMCP-1) on the surface of sensitized mast cells, along with decreased FcϵRI+ and c-kit+ expression. The levels of Th2-related cytokines (IL-4, IL-5, IL-13) decreased and that of a Th1-related cytokine (IFN-Î) increased slightly, which suggests that conjugation with QUE modulated the imbalance of the Th1/Th2 immune response. Conjugation of OVA with QUE could reduce OVA allergenicity in vitro and in vivo, which could provide information for reducing food allergenicity by conjugation with polyphenols. Copyright © 2020 American Chemical Society.",
publisher = "American Chemical Society",
journal = "Journal of Agricultural and Food Chemistry",
title = "Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin",
volume = "68",
number = "13",
pages = "4027-4035",
doi = "10.1021/acs.jafc.0c00461"
}
Zhang, T., Hu, Z., Cheng, Y., Xu, H., Ćirković-Veličković, T., He, K., Sun, F., He, Z., Liu, Z.,& Wu, X.. (2020). Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin. in Journal of Agricultural and Food Chemistry
American Chemical Society., 68(13), 4027-4035.
https://doi.org/10.1021/acs.jafc.0c00461
Zhang T, Hu Z, Cheng Y, Xu H, Ćirković-Veličković T, He K, Sun F, He Z, Liu Z, Wu X. Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin. in Journal of Agricultural and Food Chemistry. 2020;68(13):4027-4035.
doi:10.1021/acs.jafc.0c00461 .
Zhang, Tingting, Hu, Zongyi, Cheng, Yongwei, Xu, Haoxie, Ćirković-Veličković, Tanja, He, Kan, Sun, Fan, He, Zhendan, Liu, Zhigang, Wu, Xuli, "Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin" in Journal of Agricultural and Food Chemistry, 68, no. 13 (2020):4027-4035,
https://doi.org/10.1021/acs.jafc.0c00461 . .
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8

Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin

Zhang, Tingting; Hu, Zongyi; Cheng, Yongwei; Xu, Haoxie; Ćirković-Veličković, Tanja; He, Kan; Sun, Fan; He, Zhendan; Liu, Zhigang; Wu, Xuli

(American Chemical Society, 2020)

TY  - JOUR
AU  - Zhang, Tingting
AU  - Hu, Zongyi
AU  - Cheng, Yongwei
AU  - Xu, Haoxie
AU  - Ćirković-Veličković, Tanja
AU  - He, Kan
AU  - Sun, Fan
AU  - He, Zhendan
AU  - Liu, Zhigang
AU  - Wu, Xuli
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3954
AB  - A previous study demonstrated decreased allergenicity in vitro of some food allergens after conjugation with polyphenols. However, little is known about how polyphenol conjugation with food allergens affects in vivo allergenicity. We conjugated a well-known food allergen, ovalbumin (OVA), with quercetin (QUE) to assess the potential allergenicity of OVA in vitro and in vivo in a BALB/c mouse model. QUE could covalently conjugate with OVA and changed the protein structure, which might destroy and/or mask OVA epitopes. Conjugation with QUE decreased IgE binding properties and the release capacity of the conjugated OVA. In vivo, as compared with native protein, conjugation with QUE decreased the levels of IgE, IgG1, IgG, plasma histamine, and mast cell protease-1 (mMCP-1) on the surface of sensitized mast cells, along with decreased FcϵRI+ and c-kit+ expression. The levels of Th2-related cytokines (IL-4, IL-5, IL-13) decreased and that of a Th1-related cytokine (IFN-Î) increased slightly, which suggests that conjugation with QUE modulated the imbalance of the Th1/Th2 immune response. Conjugation of OVA with QUE could reduce OVA allergenicity in vitro and in vivo, which could provide information for reducing food allergenicity by conjugation with polyphenols. Copyright © 2020 American Chemical Society.
PB  - American Chemical Society
T2  - Journal of Agricultural and Food Chemistry
T1  - Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin
VL  - 68
IS  - 13
SP  - 4027
EP  - 4035
DO  - 10.1021/acs.jafc.0c00461
ER  - 
@article{
author = "Zhang, Tingting and Hu, Zongyi and Cheng, Yongwei and Xu, Haoxie and Ćirković-Veličković, Tanja and He, Kan and Sun, Fan and He, Zhendan and Liu, Zhigang and Wu, Xuli",
year = "2020",
abstract = "A previous study demonstrated decreased allergenicity in vitro of some food allergens after conjugation with polyphenols. However, little is known about how polyphenol conjugation with food allergens affects in vivo allergenicity. We conjugated a well-known food allergen, ovalbumin (OVA), with quercetin (QUE) to assess the potential allergenicity of OVA in vitro and in vivo in a BALB/c mouse model. QUE could covalently conjugate with OVA and changed the protein structure, which might destroy and/or mask OVA epitopes. Conjugation with QUE decreased IgE binding properties and the release capacity of the conjugated OVA. In vivo, as compared with native protein, conjugation with QUE decreased the levels of IgE, IgG1, IgG, plasma histamine, and mast cell protease-1 (mMCP-1) on the surface of sensitized mast cells, along with decreased FcϵRI+ and c-kit+ expression. The levels of Th2-related cytokines (IL-4, IL-5, IL-13) decreased and that of a Th1-related cytokine (IFN-Î) increased slightly, which suggests that conjugation with QUE modulated the imbalance of the Th1/Th2 immune response. Conjugation of OVA with QUE could reduce OVA allergenicity in vitro and in vivo, which could provide information for reducing food allergenicity by conjugation with polyphenols. Copyright © 2020 American Chemical Society.",
publisher = "American Chemical Society",
journal = "Journal of Agricultural and Food Chemistry",
title = "Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin",
volume = "68",
number = "13",
pages = "4027-4035",
doi = "10.1021/acs.jafc.0c00461"
}
Zhang, T., Hu, Z., Cheng, Y., Xu, H., Ćirković-Veličković, T., He, K., Sun, F., He, Z., Liu, Z.,& Wu, X.. (2020). Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin. in Journal of Agricultural and Food Chemistry
American Chemical Society., 68(13), 4027-4035.
https://doi.org/10.1021/acs.jafc.0c00461
Zhang T, Hu Z, Cheng Y, Xu H, Ćirković-Veličković T, He K, Sun F, He Z, Liu Z, Wu X. Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin. in Journal of Agricultural and Food Chemistry. 2020;68(13):4027-4035.
doi:10.1021/acs.jafc.0c00461 .
Zhang, Tingting, Hu, Zongyi, Cheng, Yongwei, Xu, Haoxie, Ćirković-Veličković, Tanja, He, Kan, Sun, Fan, He, Zhendan, Liu, Zhigang, Wu, Xuli, "Changes in Allergenicity of Ovalbumin in Vitro and in Vivo on Conjugation with Quercetin" in Journal of Agricultural and Food Chemistry, 68, no. 13 (2020):4027-4035,
https://doi.org/10.1021/acs.jafc.0c00461 . .
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8

Covalent conjugation with (−)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut

He, Weiyi; Zhang, Tingting; Ćirković-Veličković, Tanja; Li, Shuiming; Lyu, Yansi; Wang, Linlin; Yi, Jiang; Liu, Zhigang; He, Zhendan; Wu, Xuli

(Elsevier, 2020)

TY  - JOUR
AU  - He, Weiyi
AU  - Zhang, Tingting
AU  - Ćirković-Veličković, Tanja
AU  - Li, Shuiming
AU  - Lyu, Yansi
AU  - Wang, Linlin
AU  - Yi, Jiang
AU  - Liu, Zhigang
AU  - He, Zhendan
AU  - Wu, Xuli
PY  - 2020
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4053
AB  - Ara h1 is a major allergen from peanut. We investigated the effect of covalent conjugation of Ara h1 and dietary polyphenols on allergenicity and functional properties of Ara h1. Enzyme-linked immunosorbent assay revealed that the covalent conjugation of dietary polyphenols significantly reduced the IgE binding capacity of Ara h1. Covalent binding of dietary polyphenols with Ara h1 reduced histamine release by 40% in basophils. The decreased IgE binding capacity of Ara h1 could be ascribed to changes in protein conformation. The IgE epitope of Ara h1 might be blocked by polyphenols at the binding site. Analysis of pepsin digestion of Ara h1–polyphenol conjugates indicated that the covalent binding increased pepsin digestibility and reduced IgE binding capacity. Furthermore, covalent conjugation of Ara h1 with polyphenols decreased denaturation temperature and increased antioxidant activity. Ara h1 conjugated with polyphenols may be a promising approach for reducing the allergenicity of Ara h1.
PB  - Elsevier
T2  - Food Chemistry
T1  - Covalent conjugation with (−)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut
VL  - 331
SP  - 127355
DO  - 10.1016/j.foodchem.2020.127355
ER  - 
@article{
author = "He, Weiyi and Zhang, Tingting and Ćirković-Veličković, Tanja and Li, Shuiming and Lyu, Yansi and Wang, Linlin and Yi, Jiang and Liu, Zhigang and He, Zhendan and Wu, Xuli",
year = "2020",
abstract = "Ara h1 is a major allergen from peanut. We investigated the effect of covalent conjugation of Ara h1 and dietary polyphenols on allergenicity and functional properties of Ara h1. Enzyme-linked immunosorbent assay revealed that the covalent conjugation of dietary polyphenols significantly reduced the IgE binding capacity of Ara h1. Covalent binding of dietary polyphenols with Ara h1 reduced histamine release by 40% in basophils. The decreased IgE binding capacity of Ara h1 could be ascribed to changes in protein conformation. The IgE epitope of Ara h1 might be blocked by polyphenols at the binding site. Analysis of pepsin digestion of Ara h1–polyphenol conjugates indicated that the covalent binding increased pepsin digestibility and reduced IgE binding capacity. Furthermore, covalent conjugation of Ara h1 with polyphenols decreased denaturation temperature and increased antioxidant activity. Ara h1 conjugated with polyphenols may be a promising approach for reducing the allergenicity of Ara h1.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Covalent conjugation with (−)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut",
volume = "331",
pages = "127355",
doi = "10.1016/j.foodchem.2020.127355"
}
He, W., Zhang, T., Ćirković-Veličković, T., Li, S., Lyu, Y., Wang, L., Yi, J., Liu, Z., He, Z.,& Wu, X.. (2020). Covalent conjugation with (−)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut. in Food Chemistry
Elsevier., 331, 127355.
https://doi.org/10.1016/j.foodchem.2020.127355
He W, Zhang T, Ćirković-Veličković T, Li S, Lyu Y, Wang L, Yi J, Liu Z, He Z, Wu X. Covalent conjugation with (−)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut. in Food Chemistry. 2020;331:127355.
doi:10.1016/j.foodchem.2020.127355 .
He, Weiyi, Zhang, Tingting, Ćirković-Veličković, Tanja, Li, Shuiming, Lyu, Yansi, Wang, Linlin, Yi, Jiang, Liu, Zhigang, He, Zhendan, Wu, Xuli, "Covalent conjugation with (−)-epigallo-catechin 3-gallate and chlorogenic acid changes allergenicity and functional properties of Ara h1 from peanut" in Food Chemistry, 331 (2020):127355,
https://doi.org/10.1016/j.foodchem.2020.127355 . .
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