Stojadinović, Marija M.

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  • Stojadinović, Marija M. (21)
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Author's Bibliography

Supplementary material for the article: Al-Hanish, A.; Stanic-Vucinic, D.; Mihailovic, J.; Prodic, I.; Minic, S.; Stojadinovic, M.; Radibratovic, M.; Milcic, M.; Cirkovic Velickovic, T. Noncovalent Interactions of Bovine α-Lactalbumin with Green Tea Polyphenol, Epigalocatechin-3-Gallate. Food Hydrocolloids 2016, 61, 241–250. https://doi.org/10.1016/j.foodhyd.2016.05.012

Al-Hanish, Ayah; Stanić-Vučinić, Dragana; Mihailović-Vesić, Jelena; Prodić, Ivana; Minić, Simeon L.; Stojadinović, Marija M.; Radibratović, Milica; Milčić, Miloš K.; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2016)

TY  - BOOK
AU  - Al-Hanish, Ayah
AU  - Stanić-Vučinić, Dragana
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Minić, Simeon L.
AU  - Stojadinović, Marija M.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3585
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Hydrocolloids
T1  - Supplementary material for the article: Al-Hanish, A.; Stanic-Vucinic, D.; Mihailovic, J.; Prodic, I.; Minic, S.; Stojadinovic, M.; Radibratovic, M.; Milcic, M.; Cirkovic Velickovic, T. Noncovalent Interactions of Bovine α-Lactalbumin with Green Tea Polyphenol, Epigalocatechin-3-Gallate. Food Hydrocolloids 2016, 61, 241–250. https://doi.org/10.1016/j.foodhyd.2016.05.012
ER  - 
@book{
author = "Al-Hanish, Ayah and Stanić-Vučinić, Dragana and Mihailović-Vesić, Jelena and Prodić, Ivana and Minić, Simeon L. and Stojadinović, Marija M. and Radibratović, Milica and Milčić, Miloš K. and Ćirković-Veličković, Tanja",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3585",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Hydrocolloids",
title = "Supplementary material for the article: Al-Hanish, A.; Stanic-Vucinic, D.; Mihailovic, J.; Prodic, I.; Minic, S.; Stojadinovic, M.; Radibratovic, M.; Milcic, M.; Cirkovic Velickovic, T. Noncovalent Interactions of Bovine α-Lactalbumin with Green Tea Polyphenol, Epigalocatechin-3-Gallate. Food Hydrocolloids 2016, 61, 241–250. https://doi.org/10.1016/j.foodhyd.2016.05.012"
}
Al-Hanish, A., Stanić-Vučinić, D., Mihailović-Vesić, J., Prodić, I., Minić, S. L., Stojadinović, M. M., Radibratović, M., Milčić, M. K.,& Ćirković-Veličković, T. (2016). Supplementary material for the article: Al-Hanish, A.; Stanic-Vucinic, D.; Mihailovic, J.; Prodic, I.; Minic, S.; Stojadinovic, M.; Radibratovic, M.; Milcic, M.; Cirkovic Velickovic, T. Noncovalent Interactions of Bovine α-Lactalbumin with Green Tea Polyphenol, Epigalocatechin-3-Gallate. Food Hydrocolloids 2016, 61, 241–250. https://doi.org/10.1016/j.foodhyd.2016.05.012.
Food Hydrocolloids
Elsevier Sci Ltd, Oxford..
Al-Hanish A, Stanić-Vučinić D, Mihailović-Vesić J, Prodić I, Minić SL, Stojadinović MM, Radibratović M, Milčić MK, Ćirković-Veličković T. Supplementary material for the article: Al-Hanish, A.; Stanic-Vucinic, D.; Mihailovic, J.; Prodic, I.; Minic, S.; Stojadinovic, M.; Radibratovic, M.; Milcic, M.; Cirkovic Velickovic, T. Noncovalent Interactions of Bovine α-Lactalbumin with Green Tea Polyphenol, Epigalocatechin-3-Gallate. Food Hydrocolloids 2016, 61, 241–250. https://doi.org/10.1016/j.foodhyd.2016.05.012. Food Hydrocolloids. 2016;
Al-Hanish Ayah, Stanić-Vučinić Dragana, Mihailović-Vesić Jelena, Prodić Ivana, Minić Simeon L., Stojadinović Marija M., Radibratović Milica, Milčić Miloš K., Ćirković-Veličković Tanja, "Supplementary material for the article: Al-Hanish, A.; Stanic-Vucinic, D.; Mihailovic, J.; Prodic, I.; Minic, S.; Stojadinovic, M.; Radibratovic, M.; Milcic, M.; Cirkovic Velickovic, T. Noncovalent Interactions of Bovine α-Lactalbumin with Green Tea Polyphenol, Epigalocatechin-3-Gallate. Food Hydrocolloids 2016, 61, 241–250. https://doi.org/10.1016/j.foodhyd.2016.05.012" Food Hydrocolloids (2016)

Supplementary data for the article: Stanic-Vucinic, D.; Stojadinovic, M.; Mirkov, I.; Apostolovic, D.; Burazer, L.; Atanaskovic-Markovic, M.; Kataranovski, M.; Cirkovic Velickovic, T. Hypoallergenic Acid-Sensitive Modification Preserves Major Mugwort Allergen Fold and Delivers Full Repertoire of MHC Class II-Binding Peptides during Endolysosomal Degradation. RSC Advances 2016, 6 (91), 88216–88228. https://doi.org/10.1039/c6ra17261j

Stanić-Vučinić, Dragana; Stojadinović, Marija M.; Mirkov, Ivana; Apostolović, Danijela; Burazer, Lidija M.; Atanasković-Marković, Marina; Kataranovski, Milena; Ćirković-Veličković, Tanja

(Royal Soc Chemistry, Cambridge, 2016)

TY  - BOOK
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Mirkov, Ivana
AU  - Apostolović, Danijela
AU  - Burazer, Lidija M.
AU  - Atanasković-Marković, Marina
AU  - Kataranovski, Milena
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3528
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Supplementary data for the article: Stanic-Vucinic, D.; Stojadinovic, M.; Mirkov, I.; Apostolovic, D.; Burazer, L.; Atanaskovic-Markovic, M.; Kataranovski, M.; Cirkovic Velickovic, T. Hypoallergenic Acid-Sensitive Modification Preserves Major Mugwort Allergen Fold and Delivers Full Repertoire of MHC Class II-Binding Peptides during Endolysosomal Degradation. RSC Advances 2016, 6 (91), 88216–88228. https://doi.org/10.1039/c6ra17261j
ER  - 
@book{
author = "Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Mirkov, Ivana and Apostolović, Danijela and Burazer, Lidija M. and Atanasković-Marković, Marina and Kataranovski, Milena and Ćirković-Veličković, Tanja",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3528",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Supplementary data for the article: Stanic-Vucinic, D.; Stojadinovic, M.; Mirkov, I.; Apostolovic, D.; Burazer, L.; Atanaskovic-Markovic, M.; Kataranovski, M.; Cirkovic Velickovic, T. Hypoallergenic Acid-Sensitive Modification Preserves Major Mugwort Allergen Fold and Delivers Full Repertoire of MHC Class II-Binding Peptides during Endolysosomal Degradation. RSC Advances 2016, 6 (91), 88216–88228. https://doi.org/10.1039/c6ra17261j"
}
Stanić-Vučinić, D., Stojadinović, M. M., Mirkov, I., Apostolović, D., Burazer, L. M., Atanasković-Marković, M., Kataranovski, M.,& Ćirković-Veličković, T. (2016). Supplementary data for the article: Stanic-Vucinic, D.; Stojadinovic, M.; Mirkov, I.; Apostolovic, D.; Burazer, L.; Atanaskovic-Markovic, M.; Kataranovski, M.; Cirkovic Velickovic, T. Hypoallergenic Acid-Sensitive Modification Preserves Major Mugwort Allergen Fold and Delivers Full Repertoire of MHC Class II-Binding Peptides during Endolysosomal Degradation. RSC Advances 2016, 6 (91), 88216–88228. https://doi.org/10.1039/c6ra17261j.
RSC Advances
Royal Soc Chemistry, Cambridge..
Stanić-Vučinić D, Stojadinović MM, Mirkov I, Apostolović D, Burazer LM, Atanasković-Marković M, Kataranovski M, Ćirković-Veličković T. Supplementary data for the article: Stanic-Vucinic, D.; Stojadinovic, M.; Mirkov, I.; Apostolovic, D.; Burazer, L.; Atanaskovic-Markovic, M.; Kataranovski, M.; Cirkovic Velickovic, T. Hypoallergenic Acid-Sensitive Modification Preserves Major Mugwort Allergen Fold and Delivers Full Repertoire of MHC Class II-Binding Peptides during Endolysosomal Degradation. RSC Advances 2016, 6 (91), 88216–88228. https://doi.org/10.1039/c6ra17261j. RSC Advances. 2016;
Stanić-Vučinić Dragana, Stojadinović Marija M., Mirkov Ivana, Apostolović Danijela, Burazer Lidija M., Atanasković-Marković Marina, Kataranovski Milena, Ćirković-Veličković Tanja, "Supplementary data for the article: Stanic-Vucinic, D.; Stojadinovic, M.; Mirkov, I.; Apostolovic, D.; Burazer, L.; Atanaskovic-Markovic, M.; Kataranovski, M.; Cirkovic Velickovic, T. Hypoallergenic Acid-Sensitive Modification Preserves Major Mugwort Allergen Fold and Delivers Full Repertoire of MHC Class II-Binding Peptides during Endolysosomal Degradation. RSC Advances 2016, 6 (91), 88216–88228. https://doi.org/10.1039/c6ra17261j" RSC Advances (2016)

Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate

Al-Hanish, Ayah; Stanić-Vučinić, Dragana; Mihailović-Vesić, Jelena; Prodić, Ivana; Minić, Simeon L.; Stojadinović, Marija M.; Radibratović, Milica; Milčić, Miloš K.; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2016)

TY  - JOUR
AU  - Al-Hanish, Ayah
AU  - Stanić-Vučinić, Dragana
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Minić, Simeon L.
AU  - Stojadinović, Marija M.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2299
AB  - Bovine alpha-lactalbumin (ALA) is an important Ca-binding protein of milk. Epigallocatechin-3-gallate (EGCG) is the major and the most biologically active catechin of green tea, which has the highest binding affinity to whey proteins due to galloyl functional group. In this study experimental and computational methods were used to investigate noncovalent interactions of EGCG and ALA. Binding affinity of EGCG for ALA, determined by fluorescence quenching analysis, was in the range described for complexes of EGCG and other dietary proteins, and lower than affinity of some phenolic compounds to ALA. Based on circular dichroism and Fourier transform infrared spectroscopy spectra, binding of EGCG change ALA conformation inducing alpha-helix to beta-structures transition. The isothermal titration calorimetry results suggest that the binding of EGCG to ALA is enthalpically favorable. The docking analysis shows that EGCG binds in the hydrophobic pocket at the entrance of cleft between alpha-helical and beta-sheetrich domains and includes residues of aromatic cluster II. Uptake of ALA by monocytes proceeds at a slower rate in the presence of EGCG suggesting that EGCG binding may impair uptake of ALA by antigen-presenting cells. ALA, being of low cost and widely available protein, can serve as suitable delivery system for EGCG, as well as for food fortification with this bioactive catechin. (C) 2016 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Hydrocolloids
T1  - Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate
VL  - 61
SP  - 241
EP  - 250
DO  - 10.1016/j.foodhyd.2016.05.012
ER  - 
@article{
author = "Al-Hanish, Ayah and Stanić-Vučinić, Dragana and Mihailović-Vesić, Jelena and Prodić, Ivana and Minić, Simeon L. and Stojadinović, Marija M. and Radibratović, Milica and Milčić, Miloš K. and Ćirković-Veličković, Tanja",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2299",
abstract = "Bovine alpha-lactalbumin (ALA) is an important Ca-binding protein of milk. Epigallocatechin-3-gallate (EGCG) is the major and the most biologically active catechin of green tea, which has the highest binding affinity to whey proteins due to galloyl functional group. In this study experimental and computational methods were used to investigate noncovalent interactions of EGCG and ALA. Binding affinity of EGCG for ALA, determined by fluorescence quenching analysis, was in the range described for complexes of EGCG and other dietary proteins, and lower than affinity of some phenolic compounds to ALA. Based on circular dichroism and Fourier transform infrared spectroscopy spectra, binding of EGCG change ALA conformation inducing alpha-helix to beta-structures transition. The isothermal titration calorimetry results suggest that the binding of EGCG to ALA is enthalpically favorable. The docking analysis shows that EGCG binds in the hydrophobic pocket at the entrance of cleft between alpha-helical and beta-sheetrich domains and includes residues of aromatic cluster II. Uptake of ALA by monocytes proceeds at a slower rate in the presence of EGCG suggesting that EGCG binding may impair uptake of ALA by antigen-presenting cells. ALA, being of low cost and widely available protein, can serve as suitable delivery system for EGCG, as well as for food fortification with this bioactive catechin. (C) 2016 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Hydrocolloids",
title = "Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate",
volume = "61",
pages = "241-250",
doi = "10.1016/j.foodhyd.2016.05.012"
}
Al-Hanish, A., Stanić-Vučinić, D., Mihailović-Vesić, J., Prodić, I., Minić, S. L., Stojadinović, M. M., Radibratović, M., Milčić, M. K.,& Ćirković-Veličković, T. (2016). Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate.
Food Hydrocolloids
Elsevier Sci Ltd, Oxford., 61, 241-250.
https://doi.org/10.1016/j.foodhyd.2016.05.012
Al-Hanish A, Stanić-Vučinić D, Mihailović-Vesić J, Prodić I, Minić SL, Stojadinović MM, Radibratović M, Milčić MK, Ćirković-Veličković T. Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate. Food Hydrocolloids. 2016;61:241-250
Al-Hanish Ayah, Stanić-Vučinić Dragana, Mihailović-Vesić Jelena, Prodić Ivana, Minić Simeon L., Stojadinović Marija M., Radibratović Milica, Milčić Miloš K., Ćirković-Veličković Tanja, "Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate" Food Hydrocolloids, 61 (2016):241-250,
https://doi.org/10.1016/j.foodhyd.2016.05.012 .
2
61
44
58

Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation

Stanić-Vučinić, Dragana; Stojadinović, Marija M.; Mirkov, Ivana; Apostolović, Danijela; Burazer, Lidija M.; Atanasković-Marković, Marina; Kataranovski, Milena; Ćirković-Veličković, Tanja

(Royal Soc Chemistry, Cambridge, 2016)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Mirkov, Ivana
AU  - Apostolović, Danijela
AU  - Burazer, Lidija M.
AU  - Atanasković-Marković, Marina
AU  - Kataranovski, Milena
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2321
AB  - Modified allergens are a safer and more efficient alternative to natural allergens for specific immunotherapy. As the modification of an allergen can diminish its immunogenicity due to the alteration of T-cell epitopes, in this paper we study the effects of a reversible chemical modification of Art v 1, the main allergen of mugwort pollen, on its allergenicity and immunogenicity. Modification of Art v 1 by cis-aconitylation into a polyanionic derivative (CAA) did not result in any significant structural alteration. However, IgE-binding epitopes on CAA were blocked, resulting in a reduced IgE-binding and basophil activation. Both proteins induced proliferation of CD3(+)CD4(+) T-cells in mugwort-allergic patients, but only unmodified allergens increased IL-4, IL-5 and IL-10 production. Rabbit and mouse anti-CAA antibodies exhibited cross-reactivity with native allergens and blocked human IgE-binding to Art v 1. Degradation of CAA by lysosomal fraction enzymes resulted in a similar set of peptides, harboring MHC class II-binding peptides, as unmodified proteins. Thus, cis-aconitylation modified Art v 1 had a significantly reduced allergenicity, whereas its immunogenicity was completely preserved. Acid-environment-responsive modification, which releases a full repertoire of native allergen epitopes within a particular site, can be considered a smart drug delivery system, which is able to deliver a therapeutically-effective dose in a controlled manner, and minimizes adverse side effects.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation
VL  - 6
IS  - 91
SP  - 88216
EP  - 88228
DO  - 10.1039/c6ra17261j
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Mirkov, Ivana and Apostolović, Danijela and Burazer, Lidija M. and Atanasković-Marković, Marina and Kataranovski, Milena and Ćirković-Veličković, Tanja",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2321",
abstract = "Modified allergens are a safer and more efficient alternative to natural allergens for specific immunotherapy. As the modification of an allergen can diminish its immunogenicity due to the alteration of T-cell epitopes, in this paper we study the effects of a reversible chemical modification of Art v 1, the main allergen of mugwort pollen, on its allergenicity and immunogenicity. Modification of Art v 1 by cis-aconitylation into a polyanionic derivative (CAA) did not result in any significant structural alteration. However, IgE-binding epitopes on CAA were blocked, resulting in a reduced IgE-binding and basophil activation. Both proteins induced proliferation of CD3(+)CD4(+) T-cells in mugwort-allergic patients, but only unmodified allergens increased IL-4, IL-5 and IL-10 production. Rabbit and mouse anti-CAA antibodies exhibited cross-reactivity with native allergens and blocked human IgE-binding to Art v 1. Degradation of CAA by lysosomal fraction enzymes resulted in a similar set of peptides, harboring MHC class II-binding peptides, as unmodified proteins. Thus, cis-aconitylation modified Art v 1 had a significantly reduced allergenicity, whereas its immunogenicity was completely preserved. Acid-environment-responsive modification, which releases a full repertoire of native allergen epitopes within a particular site, can be considered a smart drug delivery system, which is able to deliver a therapeutically-effective dose in a controlled manner, and minimizes adverse side effects.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation",
volume = "6",
number = "91",
pages = "88216-88228",
doi = "10.1039/c6ra17261j"
}
Stanić-Vučinić, D., Stojadinović, M. M., Mirkov, I., Apostolović, D., Burazer, L. M., Atanasković-Marković, M., Kataranovski, M.,& Ćirković-Veličković, T. (2016). Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation.
RSC Advances
Royal Soc Chemistry, Cambridge., 6(91), 88216-88228.
https://doi.org/10.1039/c6ra17261j
Stanić-Vučinić D, Stojadinović MM, Mirkov I, Apostolović D, Burazer LM, Atanasković-Marković M, Kataranovski M, Ćirković-Veličković T. Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation. RSC Advances. 2016;6(91):88216-88228
Stanić-Vučinić Dragana, Stojadinović Marija M., Mirkov Ivana, Apostolović Danijela, Burazer Lidija M., Atanasković-Marković Marina, Kataranovski Milena, Ćirković-Veličković Tanja, "Hypoallergenic acid-sensitive modification preserves major mugwort allergen fold and delivers full repertoire of MHC class II-binding peptides during endolysosomal degradation" RSC Advances, 6, no. 91 (2016):88216-88228,
https://doi.org/10.1039/c6ra17261j .
1
1
1

Supplementary data for article: Krstić-Ristivojević, M.; Stojadinović, M. M.; Smiljanić, K.; Stanić-Vučinić, D.; Ćirković-Veličković, T. The Anti-Cancer Activity of Green Tea, Coffee and Cocoa Extracts on Human Cervical Adenocarcinoma HeLa Cells Depends on Both pro-Oxidant and Anti-Proliferative Activities of Polyphenols. RSC Advances 2015, 5 (5), 3260–3268. https://doi.org/10.1039/c4ra13230k

Krstić-Ristivojević, Maja; Stojadinović, Marija M.; Smiljanić, Katarina; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Royal Soc Chemistry, Cambridge, 2015)

TY  - BOOK
AU  - Krstić-Ristivojević, Maja
AU  - Stojadinović, Marija M.
AU  - Smiljanić, Katarina
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3449
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - Supplementary data for article: Krstić-Ristivojević, M.; Stojadinović, M. M.; Smiljanić, K.; Stanić-Vučinić, D.; Ćirković-Veličković, T. The Anti-Cancer Activity of Green Tea, Coffee and Cocoa Extracts on Human Cervical Adenocarcinoma HeLa Cells Depends on Both pro-Oxidant and Anti-Proliferative Activities of Polyphenols. RSC Advances 2015, 5 (5), 3260–3268. https://doi.org/10.1039/c4ra13230k
ER  - 
@book{
author = "Krstić-Ristivojević, Maja and Stojadinović, Marija M. and Smiljanić, Katarina and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2015",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3449",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "Supplementary data for article: Krstić-Ristivojević, M.; Stojadinović, M. M.; Smiljanić, K.; Stanić-Vučinić, D.; Ćirković-Veličković, T. The Anti-Cancer Activity of Green Tea, Coffee and Cocoa Extracts on Human Cervical Adenocarcinoma HeLa Cells Depends on Both pro-Oxidant and Anti-Proliferative Activities of Polyphenols. RSC Advances 2015, 5 (5), 3260–3268. https://doi.org/10.1039/c4ra13230k"
}
Krstić-Ristivojević, M., Stojadinović, M. M., Smiljanić, K., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2015). Supplementary data for article: Krstić-Ristivojević, M.; Stojadinović, M. M.; Smiljanić, K.; Stanić-Vučinić, D.; Ćirković-Veličković, T. The Anti-Cancer Activity of Green Tea, Coffee and Cocoa Extracts on Human Cervical Adenocarcinoma HeLa Cells Depends on Both pro-Oxidant and Anti-Proliferative Activities of Polyphenols. RSC Advances 2015, 5 (5), 3260–3268. https://doi.org/10.1039/c4ra13230k.
RSC Advances
Royal Soc Chemistry, Cambridge..
Krstić-Ristivojević M, Stojadinović MM, Smiljanić K, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary data for article: Krstić-Ristivojević, M.; Stojadinović, M. M.; Smiljanić, K.; Stanić-Vučinić, D.; Ćirković-Veličković, T. The Anti-Cancer Activity of Green Tea, Coffee and Cocoa Extracts on Human Cervical Adenocarcinoma HeLa Cells Depends on Both pro-Oxidant and Anti-Proliferative Activities of Polyphenols. RSC Advances 2015, 5 (5), 3260–3268. https://doi.org/10.1039/c4ra13230k. RSC Advances. 2015;
Krstić-Ristivojević Maja, Stojadinović Marija M., Smiljanić Katarina, Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Supplementary data for article: Krstić-Ristivojević, M.; Stojadinović, M. M.; Smiljanić, K.; Stanić-Vučinić, D.; Ćirković-Veličković, T. The Anti-Cancer Activity of Green Tea, Coffee and Cocoa Extracts on Human Cervical Adenocarcinoma HeLa Cells Depends on Both pro-Oxidant and Anti-Proliferative Activities of Polyphenols. RSC Advances 2015, 5 (5), 3260–3268. https://doi.org/10.1039/c4ra13230k" RSC Advances (2015)

The anti-cancer activity of green tea, coffee and cocoa extracts on human cervical adenocarcinoma HeLa cells depends on both pro-oxidant and anti-proliferative activities of polyphenols

Krstić-Ristivojević, Maja; Stojadinović, Marija M.; Smiljanić, Katarina; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Royal Soc Chemistry, Cambridge, 2015)

TY  - JOUR
AU  - Krstić-Ristivojević, Maja
AU  - Stojadinović, Marija M.
AU  - Smiljanić, Katarina
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1888
AB  - It has been shown before that dietary polyphenols possess cancer chemopreventive effects. As cervical cancer is the second leading genital malignancy in women after breast cancer, the anti-cervical cancer effects of polyphenol extracts of commonly used beverages (green tea, coffee and cocoa) were tested and compared in HeLa cells. All the extracts induced apoptosis of HeLa cells, but green tea was the most potent. However, as opposed to green tea which induced a strong anti-proliferative response in HeLa cells, coffee and cocoa extracts promoted the proliferation of surviving cells. After short-term exposure, green tea and coffee extracts, but not cocoa, induced the formation of intracellular reactive oxygen species. Only the green tea extract increased the production of superoxide anion radicals and decreased reduced glutathione levels. Gene expression of Cu/Zn and Mn-superoxide dismutase or catalase was unaltered in cells treated with extracts, but green tea partially inhibited catalase activity. The cytotoxic activity of green tea and coffee extracts was partially inhibited by vitamin C. The in vitro anti-cervical cancer potency of tested polyphenol extracts is related to their pro-oxidant and anti-proliferative activities and are exhibited in the following order: green tea  gt  coffee  gt  cocoa, with only green tea showing both pro-oxidative and anti-proliferative action.
PB  - Royal Soc Chemistry, Cambridge
T2  - RSC Advances
T1  - The anti-cancer activity of green tea, coffee and cocoa extracts on human cervical adenocarcinoma HeLa cells depends on both pro-oxidant and anti-proliferative activities of polyphenols
VL  - 5
IS  - 5
SP  - 3260
EP  - 3268
DO  - 10.1039/c4ra13230k
ER  - 
@article{
author = "Krstić-Ristivojević, Maja and Stojadinović, Marija M. and Smiljanić, Katarina and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2015",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1888",
abstract = "It has been shown before that dietary polyphenols possess cancer chemopreventive effects. As cervical cancer is the second leading genital malignancy in women after breast cancer, the anti-cervical cancer effects of polyphenol extracts of commonly used beverages (green tea, coffee and cocoa) were tested and compared in HeLa cells. All the extracts induced apoptosis of HeLa cells, but green tea was the most potent. However, as opposed to green tea which induced a strong anti-proliferative response in HeLa cells, coffee and cocoa extracts promoted the proliferation of surviving cells. After short-term exposure, green tea and coffee extracts, but not cocoa, induced the formation of intracellular reactive oxygen species. Only the green tea extract increased the production of superoxide anion radicals and decreased reduced glutathione levels. Gene expression of Cu/Zn and Mn-superoxide dismutase or catalase was unaltered in cells treated with extracts, but green tea partially inhibited catalase activity. The cytotoxic activity of green tea and coffee extracts was partially inhibited by vitamin C. The in vitro anti-cervical cancer potency of tested polyphenol extracts is related to their pro-oxidant and anti-proliferative activities and are exhibited in the following order: green tea  gt  coffee  gt  cocoa, with only green tea showing both pro-oxidative and anti-proliferative action.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "RSC Advances",
title = "The anti-cancer activity of green tea, coffee and cocoa extracts on human cervical adenocarcinoma HeLa cells depends on both pro-oxidant and anti-proliferative activities of polyphenols",
volume = "5",
number = "5",
pages = "3260-3268",
doi = "10.1039/c4ra13230k"
}
Krstić-Ristivojević, M., Stojadinović, M. M., Smiljanić, K., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2015). The anti-cancer activity of green tea, coffee and cocoa extracts on human cervical adenocarcinoma HeLa cells depends on both pro-oxidant and anti-proliferative activities of polyphenols.
RSC Advances
Royal Soc Chemistry, Cambridge., 5(5), 3260-3268.
https://doi.org/10.1039/c4ra13230k
Krstić-Ristivojević M, Stojadinović MM, Smiljanić K, Stanić-Vučinić D, Ćirković-Veličković T. The anti-cancer activity of green tea, coffee and cocoa extracts on human cervical adenocarcinoma HeLa cells depends on both pro-oxidant and anti-proliferative activities of polyphenols. RSC Advances. 2015;5(5):3260-3268
Krstić-Ristivojević Maja, Stojadinović Marija M., Smiljanić Katarina, Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "The anti-cancer activity of green tea, coffee and cocoa extracts on human cervical adenocarcinoma HeLa cells depends on both pro-oxidant and anti-proliferative activities of polyphenols" RSC Advances, 5, no. 5 (2015):3260-3268,
https://doi.org/10.1039/c4ra13230k .
1
19
19
17

Green tea, coffee and cocoa polyphenols exhibit different effects on HeLa cell viability and proliferation

Krstić-Ristivojević, Maja; Stojadinović, Marija M.; Smiljanić, Katarina; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Wiley-Blackwell, Hoboken, 2014)

TY  - CONF
AU  - Krstić-Ristivojević, Maja
AU  - Stojadinović, Marija M.
AU  - Smiljanić, Katarina
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1754
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal / Federation of European of Biochemical Societies
T1  - Green tea, coffee and cocoa polyphenols exhibit different effects on HeLa cell viability and proliferation
VL  - 281
SP  - 72
EP  - 72
ER  - 
@conference{
author = "Krstić-Ristivojević, Maja and Stojadinović, Marija M. and Smiljanić, Katarina and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2014",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1754",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal / Federation of European of Biochemical Societies",
title = "Green tea, coffee and cocoa polyphenols exhibit different effects on HeLa cell viability and proliferation",
volume = "281",
pages = "72-72"
}
Krstić-Ristivojević, M., Stojadinović, M. M., Smiljanić, K., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2014). Green tea, coffee and cocoa polyphenols exhibit different effects on HeLa cell viability and proliferation.
FEBS Journal / Federation of European of Biochemical Societies
Wiley-Blackwell, Hoboken., 281, 72-72.
Krstić-Ristivojević M, Stojadinović MM, Smiljanić K, Stanić-Vučinić D, Ćirković-Veličković T. Green tea, coffee and cocoa polyphenols exhibit different effects on HeLa cell viability and proliferation. FEBS Journal / Federation of European of Biochemical Societies. 2014;281:72-72
Krstić-Ristivojević Maja, Stojadinović Marija M., Smiljanić Katarina, Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Green tea, coffee and cocoa polyphenols exhibit different effects on HeLa cell viability and proliferation" FEBS Journal / Federation of European of Biochemical Societies, 281 (2014):72-72

Assessing immunogenicity of enzymatically cross-linked beta-lactoglobulin using dendritic-cell derived endolysosomal degradome

Stojadinović, Marija M.; Pieters, Raymond; Smit, Joost; Ćirković-Veličković, Tanja

(Wiley-Blackwell, Hoboken, 2014)

TY  - CONF
AU  - Stojadinović, Marija M.
AU  - Pieters, Raymond
AU  - Smit, Joost
AU  - Ćirković-Veličković, Tanja
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1755
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal / Federation of European of Biochemical Societies
T1  - Assessing immunogenicity of enzymatically cross-linked beta-lactoglobulin using dendritic-cell derived endolysosomal degradome
VL  - 281
SP  - 98
EP  - 98
ER  - 
@conference{
author = "Stojadinović, Marija M. and Pieters, Raymond and Smit, Joost and Ćirković-Veličković, Tanja",
year = "2014",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1755",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal / Federation of European of Biochemical Societies",
title = "Assessing immunogenicity of enzymatically cross-linked beta-lactoglobulin using dendritic-cell derived endolysosomal degradome",
volume = "281",
pages = "98-98"
}
Stojadinović, M. M., Pieters, R., Smit, J.,& Ćirković-Veličković, T. (2014). Assessing immunogenicity of enzymatically cross-linked beta-lactoglobulin using dendritic-cell derived endolysosomal degradome.
FEBS Journal / Federation of European of Biochemical Societies
Wiley-Blackwell, Hoboken., 281, 98-98.
Stojadinović MM, Pieters R, Smit J, Ćirković-Veličković T. Assessing immunogenicity of enzymatically cross-linked beta-lactoglobulin using dendritic-cell derived endolysosomal degradome. FEBS Journal / Federation of European of Biochemical Societies. 2014;281:98-98
Stojadinović Marija M., Pieters Raymond, Smit Joost, Ćirković-Veličković Tanja, "Assessing immunogenicity of enzymatically cross-linked beta-lactoglobulin using dendritic-cell derived endolysosomal degradome" FEBS Journal / Federation of European of Biochemical Societies, 281 (2014):98-98

Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white

Ognjenović, Jana; Stojadinović, Marija M.; Milčić, Miloš K.; Apostolović, Danijela; Mihailović-Vesić, Jelena; Stambolić, Ivan; Atanasković-Marković, Marina; Simonovic, Miljan; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2014)

TY  - JOUR
AU  - Ognjenović, Jana
AU  - Stojadinović, Marija M.
AU  - Milčić, Miloš K.
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Stambolić, Ivan
AU  - Atanasković-Marković, Marina
AU  - Simonovic, Miljan
AU  - Ćirković-Veličković, Tanja
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1820
AB  - Polyphenols, the potent plant secondary metabolites, have beneficial effects on human health, but the mechanism(s) by which these effects are exerted is not well understood. Here, we present the detailed analysis of the interactions between the major green tea catechin, epigallo-catechin 3-gallate (EGCG), and the major dietary protein and allergen, ovalbumin (OVA). We show that EGCG binds to the pocket that partly overlaps with the previously identified IgE-binding region in OVA, and that this interaction induces structural changes in the allergen. Moreover, our ex vivo studies reveal that OVA binds IgE and stimulates degranulation of basophils, and that its uptake by monocytes proceeds at a slower rate in the presence of EGCG. This study provides further evidence in support of the proposed mechanism by which EGCG interactions with the food allergens contribute to its diverse biological activities and may impair antigen uptake by antigen-presenting cells. (C) 2014 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white
VL  - 164
SP  - 36
EP  - 43
DO  - 10.1016/j.foodchem.2014.05.005
ER  - 
@article{
author = "Ognjenović, Jana and Stojadinović, Marija M. and Milčić, Miloš K. and Apostolović, Danijela and Mihailović-Vesić, Jelena and Stambolić, Ivan and Atanasković-Marković, Marina and Simonovic, Miljan and Ćirković-Veličković, Tanja",
year = "2014",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1820",
abstract = "Polyphenols, the potent plant secondary metabolites, have beneficial effects on human health, but the mechanism(s) by which these effects are exerted is not well understood. Here, we present the detailed analysis of the interactions between the major green tea catechin, epigallo-catechin 3-gallate (EGCG), and the major dietary protein and allergen, ovalbumin (OVA). We show that EGCG binds to the pocket that partly overlaps with the previously identified IgE-binding region in OVA, and that this interaction induces structural changes in the allergen. Moreover, our ex vivo studies reveal that OVA binds IgE and stimulates degranulation of basophils, and that its uptake by monocytes proceeds at a slower rate in the presence of EGCG. This study provides further evidence in support of the proposed mechanism by which EGCG interactions with the food allergens contribute to its diverse biological activities and may impair antigen uptake by antigen-presenting cells. (C) 2014 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white",
volume = "164",
pages = "36-43",
doi = "10.1016/j.foodchem.2014.05.005"
}
Ognjenović, J., Stojadinović, M. M., Milčić, M. K., Apostolović, D., Mihailović-Vesić, J., Stambolić, I., Atanasković-Marković, M., Simonovic, M.,& Ćirković-Veličković, T. (2014). Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white.
Food Chemistry
Elsevier Sci Ltd, Oxford., 164, 36-43.
https://doi.org/10.1016/j.foodchem.2014.05.005
Ognjenović J, Stojadinović MM, Milčić MK, Apostolović D, Mihailović-Vesić J, Stambolić I, Atanasković-Marković M, Simonovic M, Ćirković-Veličković T. Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white. Food Chemistry. 2014;164:36-43
Ognjenović Jana, Stojadinović Marija M., Milčić Miloš K., Apostolović Danijela, Mihailović-Vesić Jelena, Stambolić Ivan, Atanasković-Marković Marina, Simonovic Miljan, Ćirković-Veličković Tanja, "Interactions of epigallo-catechin 3-gallate and ovalbumin, the major allergen of egg white" Food Chemistry, 164 (2014):36-43,
https://doi.org/10.1016/j.foodchem.2014.05.005 .
1
49
43
45

Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing

Stojadinović, Marija M.; Pieters, Raymond; Smit, Joost; Ćirković-Veličković, Tanja

(Oxford Univ Press, Oxford, 2014)

TY  - JOUR
AU  - Stojadinović, Marija M.
AU  - Pieters, Raymond
AU  - Smit, Joost
AU  - Ćirković-Veličković, Tanja
PY  - 2014
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1823
AB  - Cross-linking of proteins has been exploited by the food industry to change food texture and functionality but the effects of these manipulations on food allergenicity still remain unclear. To model the safety assessment of these food biopolymers, we created cross-linked bovine beta-lactoglobulin (CL-BLG) by laccase treatment. The purpose of the present study was to compare the immunogenicity and allergenicity of CL-BLG with native BLG in a mouse model of food allergy. First, BALB/c mice were intragastrically sensitized and orally challenged with BLG or CL-BLG and BLG-specific serum antibodies and splenic leukocyte cytokine production and cell proliferation were measured. Hereafter, epithelial protein uptake was monitored in vitro and in vivo and the effects of BLG cross-linking on interactions with dendritic cells were analyzed in vitro. Sensitization of mice with CL-BLG resulted in higher levels of IgE, IgG1, and IgG2a. In contrast, a subsequent oral challenge with CL-BLG resulted in lower mast cell degranulation. Cross-linking of BLG reduced its epithelial uptake but promoted sampling through Peyer's patches. Differences in endocytosis by dendritic cells (DCs) and in vitro endolysosomal processing were observed between BLG and CL-BLG. CL-BLG primed DCs induced higher Th2 response in vitro. Cross-linking of BLG increased its sensitizing capacity, implying that the assessment of highly polymerized food proteins is of clinical importance in food allergy. Moreover, manufacturers of foods or therapeutic proteins should pay considerate attention to the health risk of protein aggregation.
PB  - Oxford Univ Press, Oxford
T2  - Toxicological Sciences
T1  - Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing
VL  - 140
IS  - 1
SP  - 224
EP  - 235
DO  - 10.1093/toxsci/kfu062
ER  - 
@article{
author = "Stojadinović, Marija M. and Pieters, Raymond and Smit, Joost and Ćirković-Veličković, Tanja",
year = "2014",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1823",
abstract = "Cross-linking of proteins has been exploited by the food industry to change food texture and functionality but the effects of these manipulations on food allergenicity still remain unclear. To model the safety assessment of these food biopolymers, we created cross-linked bovine beta-lactoglobulin (CL-BLG) by laccase treatment. The purpose of the present study was to compare the immunogenicity and allergenicity of CL-BLG with native BLG in a mouse model of food allergy. First, BALB/c mice were intragastrically sensitized and orally challenged with BLG or CL-BLG and BLG-specific serum antibodies and splenic leukocyte cytokine production and cell proliferation were measured. Hereafter, epithelial protein uptake was monitored in vitro and in vivo and the effects of BLG cross-linking on interactions with dendritic cells were analyzed in vitro. Sensitization of mice with CL-BLG resulted in higher levels of IgE, IgG1, and IgG2a. In contrast, a subsequent oral challenge with CL-BLG resulted in lower mast cell degranulation. Cross-linking of BLG reduced its epithelial uptake but promoted sampling through Peyer's patches. Differences in endocytosis by dendritic cells (DCs) and in vitro endolysosomal processing were observed between BLG and CL-BLG. CL-BLG primed DCs induced higher Th2 response in vitro. Cross-linking of BLG increased its sensitizing capacity, implying that the assessment of highly polymerized food proteins is of clinical importance in food allergy. Moreover, manufacturers of foods or therapeutic proteins should pay considerate attention to the health risk of protein aggregation.",
publisher = "Oxford Univ Press, Oxford",
journal = "Toxicological Sciences",
title = "Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing",
volume = "140",
number = "1",
pages = "224-235",
doi = "10.1093/toxsci/kfu062"
}
Stojadinović, M. M., Pieters, R., Smit, J.,& Ćirković-Veličković, T. (2014). Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing.
Toxicological Sciences
Oxford Univ Press, Oxford., 140(1), 224-235.
https://doi.org/10.1093/toxsci/kfu062
Stojadinović MM, Pieters R, Smit J, Ćirković-Veličković T. Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing. Toxicological Sciences. 2014;140(1):224-235
Stojadinović Marija M., Pieters Raymond, Smit Joost, Ćirković-Veličković Tanja, "Cross-Linking of beta-Lactoglobulin Enhances Allergic Sensitization Through Changes in Cellular Uptake and Processing" Toxicological Sciences, 140, no. 1 (2014):224-235,
https://doi.org/10.1093/toxsci/kfu062 .
2
40
33
40

Supplementary data for the article: Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Binding Affinity between Dietary Polyphenols and β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chemistry 2013, 136 (3–4), 1263–1271. https://doi.org/10.1016/j.foodchem.2012.09.040

Stojadinović, Marija M.; Radosavljević, Jelena; Ognjenović, Jana; Mihailović-Vesić, Jelena; Prodić, Ivana; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2013)

TY  - BOOK
AU  - Stojadinović, Marija M.
AU  - Radosavljević, Jelena
AU  - Ognjenović, Jana
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2905
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Supplementary data for the article: Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Binding Affinity between Dietary Polyphenols and β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chemistry 2013, 136 (3–4), 1263–1271. https://doi.org/10.1016/j.foodchem.2012.09.040
ER  - 
@book{
author = "Stojadinović, Marija M. and Radosavljević, Jelena and Ognjenović, Jana and Mihailović-Vesić, Jelena and Prodić, Ivana and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2013",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2905",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Supplementary data for the article: Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Binding Affinity between Dietary Polyphenols and β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chemistry 2013, 136 (3–4), 1263–1271. https://doi.org/10.1016/j.foodchem.2012.09.040"
}
Stojadinović, M. M., Radosavljević, J., Ognjenović, J., Mihailović-Vesić, J., Prodić, I., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2013). Supplementary data for the article: Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Binding Affinity between Dietary Polyphenols and β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chemistry 2013, 136 (3–4), 1263–1271. https://doi.org/10.1016/j.foodchem.2012.09.040.
Food Chemistry
Elsevier Sci Ltd, Oxford..
Stojadinović MM, Radosavljević J, Ognjenović J, Mihailović-Vesić J, Prodić I, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary data for the article: Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Binding Affinity between Dietary Polyphenols and β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chemistry 2013, 136 (3–4), 1263–1271. https://doi.org/10.1016/j.foodchem.2012.09.040. Food Chemistry. 2013;
Stojadinović Marija M., Radosavljević Jelena, Ognjenović Jana, Mihailović-Vesić Jelena, Prodić Ivana, Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Supplementary data for the article: Stojadinovic, M.; Radosavljevic, J.; Ognjenovic, J.; Vesic, J.; Prodic, I.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Binding Affinity between Dietary Polyphenols and β-Lactoglobulin Negatively Correlates with the Protein Susceptibility to Digestion and Total Antioxidant Activity of Complexes Formed. Food Chemistry 2013, 136 (3–4), 1263–1271. https://doi.org/10.1016/j.foodchem.2012.09.040" Food Chemistry (2013)

Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed

Stojadinović, Marija M.; Radosavljević, Jelena; Ognjenović, Jana; Mihailović-Vesić, Jelena; Prodić, Ivana; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2013)

TY  - JOUR
AU  - Stojadinović, Marija M.
AU  - Radosavljević, Jelena
AU  - Ognjenović, Jana
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1577
AB  - Non-covalent interactions between beta-lactoglobulin (BLG) and polyphenol extracts of teas, coffee and cocoa were studied by fluorescence and CD spectroscopy at pH values of the gastrointestinal tract (GIT). The biological implications of non-covalent binding of polyphenols to BLG were investigated by in vitro pepsin and pancreatin digestibility assay and ABTS radical scavenging activity of complexes formed. The polyphenol-BLG systems were stable at pH values of the GIT. The most profound effect of pH on binding affinity was observed for polyphenol extracts rich in phenolic acids. Stronger non-covalent interactions delayed pepsin and pancreatin digestion of BLG and induced beta-sheet to alpha-helix transition at neutral pH. All polyphenols tested protected protein secondary structure at an extremely acidic pH of 1.2. A positive correlation was found between the strength of protein-polyphenol interactions and (a) half time of protein decay in gastric conditions (R-2 = 0.85), (b) masking of total antioxidant capacity of protein-polyphenol complexes (R-2 = 0.95).
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed
VL  - 136
IS  - 3-4
SP  - 1263
EP  - 1271
DO  - 10.1016/j.foodchem.2012.09.040
ER  - 
@article{
author = "Stojadinović, Marija M. and Radosavljević, Jelena and Ognjenović, Jana and Mihailović-Vesić, Jelena and Prodić, Ivana and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2013",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1577",
abstract = "Non-covalent interactions between beta-lactoglobulin (BLG) and polyphenol extracts of teas, coffee and cocoa were studied by fluorescence and CD spectroscopy at pH values of the gastrointestinal tract (GIT). The biological implications of non-covalent binding of polyphenols to BLG were investigated by in vitro pepsin and pancreatin digestibility assay and ABTS radical scavenging activity of complexes formed. The polyphenol-BLG systems were stable at pH values of the GIT. The most profound effect of pH on binding affinity was observed for polyphenol extracts rich in phenolic acids. Stronger non-covalent interactions delayed pepsin and pancreatin digestion of BLG and induced beta-sheet to alpha-helix transition at neutral pH. All polyphenols tested protected protein secondary structure at an extremely acidic pH of 1.2. A positive correlation was found between the strength of protein-polyphenol interactions and (a) half time of protein decay in gastric conditions (R-2 = 0.85), (b) masking of total antioxidant capacity of protein-polyphenol complexes (R-2 = 0.95).",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed",
volume = "136",
number = "3-4",
pages = "1263-1271",
doi = "10.1016/j.foodchem.2012.09.040"
}
Stojadinović, M. M., Radosavljević, J., Ognjenović, J., Mihailović-Vesić, J., Prodić, I., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2013). Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed.
Food Chemistry
Elsevier Sci Ltd, Oxford., 136(3-4), 1263-1271.
https://doi.org/10.1016/j.foodchem.2012.09.040
Stojadinović MM, Radosavljević J, Ognjenović J, Mihailović-Vesić J, Prodić I, Stanić-Vučinić D, Ćirković-Veličković T. Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed. Food Chemistry. 2013;136(3-4):1263-1271
Stojadinović Marija M., Radosavljević Jelena, Ognjenović Jana, Mihailović-Vesić Jelena, Prodić Ivana, Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed" Food Chemistry, 136, no. 3-4 (2013):1263-1271,
https://doi.org/10.1016/j.foodchem.2012.09.040 .
130
106
130

Effect of enzymatic cross-linking on allergenic properties of bovine beta-lactoglobulin

Stojadinović, Marija M.; Ćirković-Veličković, Tanja; Pieters, Raymond; Smit, Joost

(Wiley-Blackwell, Hoboken, 2013)

TY  - CONF
AU  - Stojadinović, Marija M.
AU  - Ćirković-Veličković, Tanja
AU  - Pieters, Raymond
AU  - Smit, Joost
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1417
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal / Federation of European of Biochemical Societies
T1  - Effect of enzymatic cross-linking on allergenic properties of bovine beta-lactoglobulin
VL  - 280
SP  - 467
EP  - 467
ER  - 
@conference{
author = "Stojadinović, Marija M. and Ćirković-Veličković, Tanja and Pieters, Raymond and Smit, Joost",
year = "2013",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1417",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal / Federation of European of Biochemical Societies",
title = "Effect of enzymatic cross-linking on allergenic properties of bovine beta-lactoglobulin",
volume = "280",
pages = "467-467"
}
Stojadinović, M. M., Ćirković-Veličković, T., Pieters, R.,& Smit, J. (2013). Effect of enzymatic cross-linking on allergenic properties of bovine beta-lactoglobulin.
FEBS Journal / Federation of European of Biochemical Societies
Wiley-Blackwell, Hoboken., 280, 467-467.
Stojadinović MM, Ćirković-Veličković T, Pieters R, Smit J. Effect of enzymatic cross-linking on allergenic properties of bovine beta-lactoglobulin. FEBS Journal / Federation of European of Biochemical Societies. 2013;280:467-467
Stojadinović Marija M., Ćirković-Veličković Tanja, Pieters Raymond, Smit Joost, "Effect of enzymatic cross-linking on allergenic properties of bovine beta-lactoglobulin" FEBS Journal / Federation of European of Biochemical Societies, 280 (2013):467-467

Strain differences in the toxicity of the vitamin K antagonist warfarin in rats

Djokic, Jelena; Ninkov, Marina; Popov-Aleksandrov, Aleksandra; Mirkov, Ivana; Subota, Vesna; Mihajlovic, Luka; Stojadinović, Marija M.; Stanić-Vučinić, Dragana; Kataranovski, Dragan; Kataranovski, Milena

(Serbian Chemical Soc, Belgrade, 2013)

TY  - JOUR
AU  - Djokic, Jelena
AU  - Ninkov, Marina
AU  - Popov-Aleksandrov, Aleksandra
AU  - Mirkov, Ivana
AU  - Subota, Vesna
AU  - Mihajlovic, Luka
AU  - Stojadinović, Marija M.
AU  - Stanić-Vučinić, Dragana
AU  - Kataranovski, Dragan
AU  - Kataranovski, Milena
PY  - 2013
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1624
AB  - Warfarin (3-(alpha-acetonylbenzy1)-4-hydroxy coumarin) is a vitamin K (VK) antagonist that inhibits vitamin K-dependent (VKD) processes, such as blood coagulation. It also exerts an influence on some non-VKD-related activities. In this study, the effect of sub-acute (30-day) oral warfarin (2 and 1 mg L-1) intake on hematological parameters was examined in two rat strains, Albino Oxford (AO) and Dark Agouti (DA), that differ in their sensitivity to certain chemicals. Greater susceptibility to the anticoagulant effect of 2 mg L-1 of warfarin was observed in AO rats and was associated with an increase in the relevant hematological parameters in this strain. Although both strains responded to 2 mg L-1 of warfarin with quantitative changes in the peripheral blood leukocytes, differential bone marrow and lung responses were observed. Strain-related differences in the pro-inflammatory activity of peripheral blood granulocytes and in mononuclear cell IFN-gamma production were observed. Recognition of differences in quantitative and qualitative effects of oral warfarin on processes other than hemostasis might be of relevance for those humans who are on warfarin therapy.
AB  - Varfarin (3-α-acetonilbenzil)-4–hidroksikumarin) je antagonist vitamina K (VK) koji inhibira procese zavisne od ovog vitamina, uključujući koagulaciju krvi. Osim toga, on ispoljava i aktivnosti koje ne zavise od vitamina K kao što su anti-tumorska i imunomodulatorna aktivnost. U ovom radu je ispitan efekat subakutnog (30 dana) oralnog unosa varfarina na hematološke parametre i aktivnost leukocita periferne krvi kod dva soja pacova Albino Oxford (AO) i Dark Agouti (DA) koji se raz- likuju u osetljivosti na iste hemijske agense. Kod jedinki AO soja zapažena je veća smrtnost nakon konzumiranja doze od 4 mg L–1 kao i veća osetljivost na antikoagulantno dejstvo varfarina pri nižim dozama (2 mg L–1) koje je praćeno povećanjem nekih hematoloških parametara. Iako kod jedinki oba soja dolazi do povećanja broja neutrofilnih leukocita periferne krvi pri dozi od 2 mg L–1, promene u osnovnim proinflamatornim aktivnostima ovih ćelija su zapažene samo kod jedinki DA soja. Promene u broju neutrofilnih leukocita u krvi DA jedinki su praćene povećanjem broja granulocitnih prekursora u koštanoj srži, dok prisustvo neutrofila u plućima AO jedinki ukazuje na razmenu ćelija između periferne krvi i plućnog intravaskularnog pula ćelija. Diferencijalne sojno–zavisne promene u aktivnosti mononuklearnih ćelija periferne krvi su takođe zapažene. Razlike u efektu oralno unetog varfarina mogu da imaju implikacije za osobe na oralnoj varfarinskoj terapiji.
PB  - Serbian Chemical Soc, Belgrade
T2  - Journal of the Serbian Chemical Society
T1  - Strain differences in the toxicity of the vitamin K antagonist warfarin in rats
T1  - Sojne razlike u toksičnosti antagoniste vitamina K varfarina kod pacova
VL  - 78
IS  - 3
SP  - 381
EP  - 394
DO  - 10.2298/JSC121114010D
ER  - 
@article{
author = "Djokic, Jelena and Ninkov, Marina and Popov-Aleksandrov, Aleksandra and Mirkov, Ivana and Subota, Vesna and Mihajlovic, Luka and Stojadinović, Marija M. and Stanić-Vučinić, Dragana and Kataranovski, Dragan and Kataranovski, Milena",
year = "2013",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1624",
abstract = "Warfarin (3-(alpha-acetonylbenzy1)-4-hydroxy coumarin) is a vitamin K (VK) antagonist that inhibits vitamin K-dependent (VKD) processes, such as blood coagulation. It also exerts an influence on some non-VKD-related activities. In this study, the effect of sub-acute (30-day) oral warfarin (2 and 1 mg L-1) intake on hematological parameters was examined in two rat strains, Albino Oxford (AO) and Dark Agouti (DA), that differ in their sensitivity to certain chemicals. Greater susceptibility to the anticoagulant effect of 2 mg L-1 of warfarin was observed in AO rats and was associated with an increase in the relevant hematological parameters in this strain. Although both strains responded to 2 mg L-1 of warfarin with quantitative changes in the peripheral blood leukocytes, differential bone marrow and lung responses were observed. Strain-related differences in the pro-inflammatory activity of peripheral blood granulocytes and in mononuclear cell IFN-gamma production were observed. Recognition of differences in quantitative and qualitative effects of oral warfarin on processes other than hemostasis might be of relevance for those humans who are on warfarin therapy., Varfarin (3-α-acetonilbenzil)-4–hidroksikumarin) je antagonist vitamina K (VK) koji inhibira procese zavisne od ovog vitamina, uključujući koagulaciju krvi. Osim toga, on ispoljava i aktivnosti koje ne zavise od vitamina K kao što su anti-tumorska i imunomodulatorna aktivnost. U ovom radu je ispitan efekat subakutnog (30 dana) oralnog unosa varfarina na hematološke parametre i aktivnost leukocita periferne krvi kod dva soja pacova Albino Oxford (AO) i Dark Agouti (DA) koji se raz- likuju u osetljivosti na iste hemijske agense. Kod jedinki AO soja zapažena je veća smrtnost nakon konzumiranja doze od 4 mg L–1 kao i veća osetljivost na antikoagulantno dejstvo varfarina pri nižim dozama (2 mg L–1) koje je praćeno povećanjem nekih hematoloških parametara. Iako kod jedinki oba soja dolazi do povećanja broja neutrofilnih leukocita periferne krvi pri dozi od 2 mg L–1, promene u osnovnim proinflamatornim aktivnostima ovih ćelija su zapažene samo kod jedinki DA soja. Promene u broju neutrofilnih leukocita u krvi DA jedinki su praćene povećanjem broja granulocitnih prekursora u koštanoj srži, dok prisustvo neutrofila u plućima AO jedinki ukazuje na razmenu ćelija između periferne krvi i plućnog intravaskularnog pula ćelija. Diferencijalne sojno–zavisne promene u aktivnosti mononuklearnih ćelija periferne krvi su takođe zapažene. Razlike u efektu oralno unetog varfarina mogu da imaju implikacije za osobe na oralnoj varfarinskoj terapiji.",
publisher = "Serbian Chemical Soc, Belgrade",
journal = "Journal of the Serbian Chemical Society",
title = "Strain differences in the toxicity of the vitamin K antagonist warfarin in rats, Sojne razlike u toksičnosti antagoniste vitamina K varfarina kod pacova",
volume = "78",
number = "3",
pages = "381-394",
doi = "10.2298/JSC121114010D"
}
Djokic, J., Ninkov, M., Popov-Aleksandrov, A., Mirkov, I., Subota, V., Mihajlovic, L., Stojadinović, M. M., Stanić-Vučinić, D., Kataranovski, D.,& Kataranovski, M. (2013). Sojne razlike u toksičnosti antagoniste vitamina K varfarina kod pacova.
Journal of the Serbian Chemical Society
Serbian Chemical Soc, Belgrade., 78(3), 381-394.
https://doi.org/10.2298/JSC121114010D
Djokic J, Ninkov M, Popov-Aleksandrov A, Mirkov I, Subota V, Mihajlovic L, Stojadinović MM, Stanić-Vučinić D, Kataranovski D, Kataranovski M. Sojne razlike u toksičnosti antagoniste vitamina K varfarina kod pacova. Journal of the Serbian Chemical Society. 2013;78(3):381-394
Djokic Jelena, Ninkov Marina, Popov-Aleksandrov Aleksandra, Mirkov Ivana, Subota Vesna, Mihajlovic Luka, Stojadinović Marija M., Stanić-Vučinić Dragana, Kataranovski Dragan, Kataranovski Milena, "Sojne razlike u toksičnosti antagoniste vitamina K varfarina kod pacova" Journal of the Serbian Chemical Society, 78, no. 3 (2013):381-394,
https://doi.org/10.2298/JSC121114010D .
3
4
4

Application of ion exchanger in the separation of whey proteins and lactin from milk whey

Stanić, Dragana; Radosavljević, Jelena; Stojadinović, Marija M.; Ćirković-Veličković, Tanja

(2012)

TY  - CHAP
AU  - Stanić, Dragana
AU  - Radosavljević, Jelena
AU  - Stojadinović, Marija M.
AU  - Ćirković-Veličković, Tanja
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/289
AB  - Whey disposal represents a huge obstacle for dairy industry, being costly and problematic. On the other hand, it could be used as a starting material for isolation of some components that are valuable on the market. Whey processing is not an easy operation; it requires robust techniques of high volumetric throughput with minimal pretreatment of the starting material. For this purpose, ion exchangers can be used, due to their versatility, safety, and relative cheapness. Being a mixture of acidic and basic proteins, double-step ion exchange chromatography, involving both cation and anion exchangers, must be performed to obtain highly purified whey proteins. Development of new technologies, based on ion exchange, which can provide fast and efficient whey processing, provides maximal exploitation in environmentally safe way. In this chapter, the literature review on the usage of ion exchangers in the separation of lactin from bovine whey proteins and fractionation of bovine whey proteins will be given. © 2012 Springer Science+Business Media B.V. All rights are reserved.
T1  - Application of ion exchanger in the separation of whey proteins and lactin from milk whey
SP  - 35
EP  - 63
DO  - 10.1007/978-94-007-4026-6_2
ER  - 
@article{
author = "Stanić, Dragana and Radosavljević, Jelena and Stojadinović, Marija M. and Ćirković-Veličković, Tanja",
year = "2012",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/289",
abstract = "Whey disposal represents a huge obstacle for dairy industry, being costly and problematic. On the other hand, it could be used as a starting material for isolation of some components that are valuable on the market. Whey processing is not an easy operation; it requires robust techniques of high volumetric throughput with minimal pretreatment of the starting material. For this purpose, ion exchangers can be used, due to their versatility, safety, and relative cheapness. Being a mixture of acidic and basic proteins, double-step ion exchange chromatography, involving both cation and anion exchangers, must be performed to obtain highly purified whey proteins. Development of new technologies, based on ion exchange, which can provide fast and efficient whey processing, provides maximal exploitation in environmentally safe way. In this chapter, the literature review on the usage of ion exchangers in the separation of lactin from bovine whey proteins and fractionation of bovine whey proteins will be given. © 2012 Springer Science+Business Media B.V. All rights are reserved.",
title = "Application of ion exchanger in the separation of whey proteins and lactin from milk whey",
pages = "35-63",
doi = "10.1007/978-94-007-4026-6_2"
}
Stanić, D., Radosavljević, J., Stojadinović, M. M.,& Ćirković-Veličković, T. (2012). Application of ion exchanger in the separation of whey proteins and lactin from milk whey.
, 35-63.
https://doi.org/10.1007/978-94-007-4026-6_2
Stanić D, Radosavljević J, Stojadinović MM, Ćirković-Veličković T. Application of ion exchanger in the separation of whey proteins and lactin from milk whey. 2012;:35-63
Stanić Dragana, Radosavljević Jelena, Stojadinović Marija M., Ćirković-Veličković Tanja, "Application of ion exchanger in the separation of whey proteins and lactin from milk whey" (2012):35-63,
https://doi.org/10.1007/978-94-007-4026-6_2 .
1
2

Non-covalent interactions between dietary polyphenols and bovine beta-lactoglobulin: Effect on the protein structure, digestibility and total antioxidant capacity

Stojadinović, Marija M.; Ognjenović, J.; Radosavljević, Jelena; Mihailović-Vesić, Jelena; Prodić, Ivana; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Wiley-Blackwell, Hoboken, 2012)

TY  - CONF
AU  - Stojadinović, Marija M.
AU  - Ognjenović, J.
AU  - Radosavljević, Jelena
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1527
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal / Federation of European of Biochemical Societies
T1  - Non-covalent interactions between dietary polyphenols and bovine beta-lactoglobulin: Effect on the protein structure, digestibility and total antioxidant capacity
VL  - 279
SP  - 400
EP  - 400
ER  - 
@conference{
author = "Stojadinović, Marija M. and Ognjenović, J. and Radosavljević, Jelena and Mihailović-Vesić, Jelena and Prodić, Ivana and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2012",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1527",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal / Federation of European of Biochemical Societies",
title = "Non-covalent interactions between dietary polyphenols and bovine beta-lactoglobulin: Effect on the protein structure, digestibility and total antioxidant capacity",
volume = "279",
pages = "400-400"
}
Stojadinović, M. M., Ognjenović, J., Radosavljević, J., Mihailović-Vesić, J., Prodić, I., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2012). Non-covalent interactions between dietary polyphenols and bovine beta-lactoglobulin: Effect on the protein structure, digestibility and total antioxidant capacity.
FEBS Journal / Federation of European of Biochemical Societies
Wiley-Blackwell, Hoboken., 279, 400-400.
Stojadinović MM, Ognjenović J, Radosavljević J, Mihailović-Vesić J, Prodić I, Stanić-Vučinić D, Ćirković-Veličković T. Non-covalent interactions between dietary polyphenols and bovine beta-lactoglobulin: Effect on the protein structure, digestibility and total antioxidant capacity. FEBS Journal / Federation of European of Biochemical Societies. 2012;279:400-400
Stojadinović Marija M., Ognjenović J., Radosavljević Jelena, Mihailović-Vesić Jelena, Prodić Ivana, Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Non-covalent interactions between dietary polyphenols and bovine beta-lactoglobulin: Effect on the protein structure, digestibility and total antioxidant capacity" FEBS Journal / Federation of European of Biochemical Societies, 279 (2012):400-400
2

One-step method for isolation and purification of native beta-lactoglobulin from bovine whey

Stojadinović, Marija M.; Burazer, Lidija M.; Ercili-Cura, Dilek; Sancho, Ana; Buchert, Johanna; Ćirković-Veličković, Tanja; Stanić-Vučinić, Dragana

(Wiley-Blackwell, Malden, 2012)

TY  - JOUR
AU  - Stojadinović, Marija M.
AU  - Burazer, Lidija M.
AU  - Ercili-Cura, Dilek
AU  - Sancho, Ana
AU  - Buchert, Johanna
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1275
AB  - BACKGROUND: The major whey protein beta-lactoglobulin (BLG) has been widely studied for its functional properties. The aim of this study was to develop an efficient, inexpensive and rapid one-step method for the isolation and purification of BLG while preserving its native structure. RESULTS: BLGwas purified fromdefattedwheyobtainedfromrawcow's milkbyanionexchangechromatography. Protein purity and identitywere determined using reverse phase high-performance liquid chromatography andmass spectrometry. Total BLG yield was 80% with protein purity from 97 to 99%. BLG isoforms A and B were separated into fractions of 91 and 99% purity respectively. The structure and native conformation of the isolated BLGwere compared with those of standard commercial BLG by circular dichroism spectrometry, susceptibility to various crosslinking enzymes and enzyme-linked immunosorbent assay inhibition. CONCLUSION: Theproposedmethodis veryuseful for the rapid preparationofBLGsuitable for studying antigenicandmolecular characteristics of this protein, aswell as the effect of food processing on these properties. The procedure requires only 1 day for the purification of about 300 mgof BLG from a single run using a small column (2.5 cmx20 cm) of diethylaminoethyl Sephadex and has potential for scaling up. (C) 2011 Society of Chemical Industry
PB  - Wiley-Blackwell, Malden
T2  - Journal of the Science of Food and Agriculture
T1  - One-step method for isolation and purification of native beta-lactoglobulin from bovine whey
VL  - 92
IS  - 7
SP  - 1432
EP  - 1440
DO  - 10.1002/jsfa.4722
ER  - 
@article{
author = "Stojadinović, Marija M. and Burazer, Lidija M. and Ercili-Cura, Dilek and Sancho, Ana and Buchert, Johanna and Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2012",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1275",
abstract = "BACKGROUND: The major whey protein beta-lactoglobulin (BLG) has been widely studied for its functional properties. The aim of this study was to develop an efficient, inexpensive and rapid one-step method for the isolation and purification of BLG while preserving its native structure. RESULTS: BLGwas purified fromdefattedwheyobtainedfromrawcow's milkbyanionexchangechromatography. Protein purity and identitywere determined using reverse phase high-performance liquid chromatography andmass spectrometry. Total BLG yield was 80% with protein purity from 97 to 99%. BLG isoforms A and B were separated into fractions of 91 and 99% purity respectively. The structure and native conformation of the isolated BLGwere compared with those of standard commercial BLG by circular dichroism spectrometry, susceptibility to various crosslinking enzymes and enzyme-linked immunosorbent assay inhibition. CONCLUSION: Theproposedmethodis veryuseful for the rapid preparationofBLGsuitable for studying antigenicandmolecular characteristics of this protein, aswell as the effect of food processing on these properties. The procedure requires only 1 day for the purification of about 300 mgof BLG from a single run using a small column (2.5 cmx20 cm) of diethylaminoethyl Sephadex and has potential for scaling up. (C) 2011 Society of Chemical Industry",
publisher = "Wiley-Blackwell, Malden",
journal = "Journal of the Science of Food and Agriculture",
title = "One-step method for isolation and purification of native beta-lactoglobulin from bovine whey",
volume = "92",
number = "7",
pages = "1432-1440",
doi = "10.1002/jsfa.4722"
}
Stojadinović, M. M., Burazer, L. M., Ercili-Cura, D., Sancho, A., Buchert, J., Ćirković-Veličković, T.,& Stanić-Vučinić, D. (2012). One-step method for isolation and purification of native beta-lactoglobulin from bovine whey.
Journal of the Science of Food and Agriculture
Wiley-Blackwell, Malden., 92(7), 1432-1440.
https://doi.org/10.1002/jsfa.4722
Stojadinović MM, Burazer LM, Ercili-Cura D, Sancho A, Buchert J, Ćirković-Veličković T, Stanić-Vučinić D. One-step method for isolation and purification of native beta-lactoglobulin from bovine whey. Journal of the Science of Food and Agriculture. 2012;92(7):1432-1440
Stojadinović Marija M., Burazer Lidija M., Ercili-Cura Dilek, Sancho Ana, Buchert Johanna, Ćirković-Veličković Tanja, Stanić-Vučinić Dragana, "One-step method for isolation and purification of native beta-lactoglobulin from bovine whey" Journal of the Science of Food and Agriculture, 92, no. 7 (2012):1432-1440,
https://doi.org/10.1002/jsfa.4722 .
18
16
17

Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound

Stanić-Vučinić, Dragana; Stojadinović, Marija M.; Atanasković-Marković, Marina; Ognjenović, Jana; Gronlund, Hans; van Hage, Marianne; Lantto, Raija; Sancho, Ana I.; Ćirković-Veličković, Tanja

(Wiley-Blackwell, Hoboken, 2012)

TY  - JOUR
AU  - Stanić-Vučinić, Dragana
AU  - Stojadinović, Marija M.
AU  - Atanasković-Marković, Marina
AU  - Ognjenović, Jana
AU  - Gronlund, Hans
AU  - van Hage, Marianne
AU  - Lantto, Raija
AU  - Sancho, Ana I.
AU  - Ćirković-Veličković, Tanja
PY  - 2012
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1561
AB  - Scope The aim of this work was to investigate the effects of high-intensity ultrasound (sonication), on the structure and allergenicity of the major cow's milk allergen, beta-lactoglobulin (BLG). Methods and results Structural changes upon sonication of BLG were monitored by circular dichroism spectroscopy, tryptophan emission fluorescence, hydrophobic dye and retinol binding, as well as digestibility and phenol-oxidase cross-linking capacity. Allergenicity was monitored in individual patients sera, basophil activation test, and skin prick testing in 41 cow's milk allergy patients. Uncontrolled local temperature changes induced modifications in BLG secondary structure accompanied by formation of dimers, trimers, and oligomers of BLG that were more digestible by pepsin and had reduced retinol binding. Controlled temperature conditions induced changes in secondary structure of BLG without causing formation of oligomers, or changing protein's capacity to bind retinol. Both sonicated forms of BLG had more exposed hydrophobic surfaces than native BLG and underwent facilitated cross-linking reaction with phenol-oxidase. Sonication had a minor effect on IgE-binding properties of BLG. Conclusion Sonication-induced structural changes in major whey allergen were not clinically significant in cow's milk allergy patients. Ultrasound can be a safe procedure for dairy processing as it maintains the nutritional value and does not increase allergenic potential of BLG.
PB  - Wiley-Blackwell, Hoboken
T2  - Molecular Nutrition and Food Research
T1  - Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound
VL  - 56
IS  - 12
SP  - 1894
EP  - 1905
DO  - 10.1002/mnfr.201200179
ER  - 
@article{
author = "Stanić-Vučinić, Dragana and Stojadinović, Marija M. and Atanasković-Marković, Marina and Ognjenović, Jana and Gronlund, Hans and van Hage, Marianne and Lantto, Raija and Sancho, Ana I. and Ćirković-Veličković, Tanja",
year = "2012",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1561",
abstract = "Scope The aim of this work was to investigate the effects of high-intensity ultrasound (sonication), on the structure and allergenicity of the major cow's milk allergen, beta-lactoglobulin (BLG). Methods and results Structural changes upon sonication of BLG were monitored by circular dichroism spectroscopy, tryptophan emission fluorescence, hydrophobic dye and retinol binding, as well as digestibility and phenol-oxidase cross-linking capacity. Allergenicity was monitored in individual patients sera, basophil activation test, and skin prick testing in 41 cow's milk allergy patients. Uncontrolled local temperature changes induced modifications in BLG secondary structure accompanied by formation of dimers, trimers, and oligomers of BLG that were more digestible by pepsin and had reduced retinol binding. Controlled temperature conditions induced changes in secondary structure of BLG without causing formation of oligomers, or changing protein's capacity to bind retinol. Both sonicated forms of BLG had more exposed hydrophobic surfaces than native BLG and underwent facilitated cross-linking reaction with phenol-oxidase. Sonication had a minor effect on IgE-binding properties of BLG. Conclusion Sonication-induced structural changes in major whey allergen were not clinically significant in cow's milk allergy patients. Ultrasound can be a safe procedure for dairy processing as it maintains the nutritional value and does not increase allergenic potential of BLG.",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Molecular Nutrition and Food Research",
title = "Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound",
volume = "56",
number = "12",
pages = "1894-1905",
doi = "10.1002/mnfr.201200179"
}
Stanić-Vučinić, D., Stojadinović, M. M., Atanasković-Marković, M., Ognjenović, J., Gronlund, H., van Hage, M., Lantto, R., Sancho, A. I.,& Ćirković-Veličković, T. (2012). Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound.
Molecular Nutrition and Food Research
Wiley-Blackwell, Hoboken., 56(12), 1894-1905.
https://doi.org/10.1002/mnfr.201200179
Stanić-Vučinić D, Stojadinović MM, Atanasković-Marković M, Ognjenović J, Gronlund H, van Hage M, Lantto R, Sancho AI, Ćirković-Veličković T. Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound. Molecular Nutrition and Food Research. 2012;56(12):1894-1905
Stanić-Vučinić Dragana, Stojadinović Marija M., Atanasković-Marković Marina, Ognjenović Jana, Gronlund Hans, van Hage Marianne, Lantto Raija, Sancho Ana I., Ćirković-Veličković Tanja, "Structural changes and allergenic properties of beta-lactoglobulin upon exposure to high-intensity ultrasound" Molecular Nutrition and Food Research, 56, no. 12 (2012):1894-1905,
https://doi.org/10.1002/mnfr.201200179 .
56
51
59

An improved method for isolation and purification of native bovine beta-lactoglobulin; separation of A and B beta-lactoglobulin isoforms

Stojadinović, Marija M.; Burazer, Lidija M.; Ercili-Cura, D.; Sancho, A.; Buchert, Johanna; Mills, C.; Ćirković-Veličković, Tanja; Stanić-Vučinić, Dragana

(Wiley-Blackwell, Hoboken, 2011)

TY  - CONF
AU  - Stojadinović, Marija M.
AU  - Burazer, Lidija M.
AU  - Ercili-Cura, D.
AU  - Sancho, A.
AU  - Buchert, Johanna
AU  - Mills, C.
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2011
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1473
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - An improved method for isolation and purification of native bovine beta-lactoglobulin; separation of A and B beta-lactoglobulin isoforms
VL  - 66
SP  - 523
EP  - 524
ER  - 
@conference{
author = "Stojadinović, Marija M. and Burazer, Lidija M. and Ercili-Cura, D. and Sancho, A. and Buchert, Johanna and Mills, C. and Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2011",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1473",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "An improved method for isolation and purification of native bovine beta-lactoglobulin; separation of A and B beta-lactoglobulin isoforms",
volume = "66",
pages = "523-524"
}
Stojadinović, M. M., Burazer, L. M., Ercili-Cura, D., Sancho, A., Buchert, J., Mills, C., Ćirković-Veličković, T.,& Stanić-Vučinić, D. (2011). An improved method for isolation and purification of native bovine beta-lactoglobulin; separation of A and B beta-lactoglobulin isoforms.
Allergy
Wiley-Blackwell, Hoboken., 66, 523-524.
Stojadinović MM, Burazer LM, Ercili-Cura D, Sancho A, Buchert J, Mills C, Ćirković-Veličković T, Stanić-Vučinić D. An improved method for isolation and purification of native bovine beta-lactoglobulin; separation of A and B beta-lactoglobulin isoforms. Allergy. 2011;66:523-524
Stojadinović Marija M., Burazer Lidija M., Ercili-Cura D., Sancho A., Buchert Johanna, Mills C., Ćirković-Veličković Tanja, Stanić-Vučinić Dragana, "An improved method for isolation and purification of native bovine beta-lactoglobulin; separation of A and B beta-lactoglobulin isoforms" Allergy, 66 (2011):523-524

Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics

Tantoush, Ziyad; Stanić, Dragana; Stojadinović, Marija M.; Ognjenović, Jana; Mihajlovic, Luka; Atanasković-Marković, Marina; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2011)

TY  - JOUR
AU  - Tantoush, Ziyad
AU  - Stanić, Dragana
AU  - Stojadinović, Marija M.
AU  - Ognjenović, Jana
AU  - Mihajlovic, Luka
AU  - Atanasković-Marković, Marina
AU  - Ćirković-Veličković, Tanja
PY  - 2011
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1137
AB  - beta-Lactoglobulin (BLG) is an important nutrient of dairy products, but it represents a serious health risk in patients allergic to milk. Sour cherry (Prunus cerasus L) extract (SCE) is frequently added as a natural food colour in composite foods, such as fruit yogurt, ice creams, frappes and milkshakes. The aim of this study was to investigate the potential of laccase to cross-link BLG in the presence of an SCE and to characterise the obtained products for their bioactivity. Laccase cross-linked BLG in the presence of sour cherry phenolics. In a basophil-activation assay, the allergenicity of the cross-linked protein was shown to decrease in all nine cow's milk-allergic patients, while digestibility of the remaining monomeric BLG in simulated conditions of the gastrointestinal tract increased. Tryptic peptides became immediately available in BLG treated by laccase and laccase/SCE. The hydrolysates obtained by trypsin digestion of BLG/laccase/SCE showed an increase of 57% in radical-scavenging activity, compared to the control BLG. Enzymatic processing and usage of natural phenolic extracts as mediators of enzymatic reaction may improve BLG safety and the availability of peptides following digestion, while conserving its bioactivity.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics
VL  - 125
IS  - 1
SP  - 84
EP  - 91
DO  - 10.1016/j.foodchem.2010.08.040
ER  - 
@article{
author = "Tantoush, Ziyad and Stanić, Dragana and Stojadinović, Marija M. and Ognjenović, Jana and Mihajlovic, Luka and Atanasković-Marković, Marina and Ćirković-Veličković, Tanja",
year = "2011",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1137",
abstract = "beta-Lactoglobulin (BLG) is an important nutrient of dairy products, but it represents a serious health risk in patients allergic to milk. Sour cherry (Prunus cerasus L) extract (SCE) is frequently added as a natural food colour in composite foods, such as fruit yogurt, ice creams, frappes and milkshakes. The aim of this study was to investigate the potential of laccase to cross-link BLG in the presence of an SCE and to characterise the obtained products for their bioactivity. Laccase cross-linked BLG in the presence of sour cherry phenolics. In a basophil-activation assay, the allergenicity of the cross-linked protein was shown to decrease in all nine cow's milk-allergic patients, while digestibility of the remaining monomeric BLG in simulated conditions of the gastrointestinal tract increased. Tryptic peptides became immediately available in BLG treated by laccase and laccase/SCE. The hydrolysates obtained by trypsin digestion of BLG/laccase/SCE showed an increase of 57% in radical-scavenging activity, compared to the control BLG. Enzymatic processing and usage of natural phenolic extracts as mediators of enzymatic reaction may improve BLG safety and the availability of peptides following digestion, while conserving its bioactivity.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics",
volume = "125",
number = "1",
pages = "84-91",
doi = "10.1016/j.foodchem.2010.08.040"
}
Tantoush, Z., Stanić, D., Stojadinović, M. M., Ognjenović, J., Mihajlovic, L., Atanasković-Marković, M.,& Ćirković-Veličković, T. (2011). Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics.
Food Chemistry
Elsevier Sci Ltd, Oxford., 125(1), 84-91.
https://doi.org/10.1016/j.foodchem.2010.08.040
Tantoush Z, Stanić D, Stojadinović MM, Ognjenović J, Mihajlovic L, Atanasković-Marković M, Ćirković-Veličković T. Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics. Food Chemistry. 2011;125(1):84-91
Tantoush Ziyad, Stanić Dragana, Stojadinović Marija M., Ognjenović Jana, Mihajlovic Luka, Atanasković-Marković Marina, Ćirković-Veličković Tanja, "Digestibility and allergenicity of beta-lactoglobulin following laccase-mediated cross-linking in the presence of sour cherry phenolics" Food Chemistry, 125, no. 1 (2011):84-91,
https://doi.org/10.1016/j.foodchem.2010.08.040 .
48
45
51

Ultrasound induced structural changes in beta-lactoglobulin decreased allergenicity and increased its digestibility

Stojadinović, Marija M.; Stanić-Vučinić, Dragana; Sancho, A.; Ćirković-Veličković, Tanja

(Wiley-Blackwell, Hoboken, 2010)

TY  - CONF
AU  - Stojadinović, Marija M.
AU  - Stanić-Vučinić, Dragana
AU  - Sancho, A.
AU  - Ćirković-Veličković, Tanja
PY  - 2010
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1466
PB  - Wiley-Blackwell, Hoboken
C3  - Allergy
T1  - Ultrasound induced structural changes in beta-lactoglobulin decreased allergenicity and increased its digestibility
VL  - 65
SP  - 183
EP  - 183
ER  - 
@conference{
author = "Stojadinović, Marija M. and Stanić-Vučinić, Dragana and Sancho, A. and Ćirković-Veličković, Tanja",
year = "2010",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1466",
publisher = "Wiley-Blackwell, Hoboken",
journal = "Allergy",
title = "Ultrasound induced structural changes in beta-lactoglobulin decreased allergenicity and increased its digestibility",
volume = "65",
pages = "183-183"
}
Stojadinović, M. M., Stanić-Vučinić, D., Sancho, A.,& Ćirković-Veličković, T. (2010). Ultrasound induced structural changes in beta-lactoglobulin decreased allergenicity and increased its digestibility.
Allergy
Wiley-Blackwell, Hoboken., 65, 183-183.
Stojadinović MM, Stanić-Vučinić D, Sancho A, Ćirković-Veličković T. Ultrasound induced structural changes in beta-lactoglobulin decreased allergenicity and increased its digestibility. Allergy. 2010;65:183-183
Stojadinović Marija M., Stanić-Vučinić Dragana, Sancho A., Ćirković-Veličković Tanja, "Ultrasound induced structural changes in beta-lactoglobulin decreased allergenicity and increased its digestibility" Allergy, 65 (2010):183-183