TY  - JOUR
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Savković, Nina
AU  - Radibratović, Milica
AU  - Mihailović-Vesić, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3186
AB  - In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions
VL  - 269
SP  - 43
EP  - 52
DO  - 10.1016/j.foodchem.2018.06.138
ER  - 

@article{
author = "Minić, Simeon L. and Radomirović, Mirjana Ž. and Savković, Nina and Radibratović, Milica and Mihailović-Vesić, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions",
volume = "269",
pages = "43-52",
doi = "10.1016/j.foodchem.2018.06.138"
}

Minić, S. L., Radomirović, M. Ž., Savković, N., Radibratović, M., Mihailović-Vesić, J., Vasović, T., Nikolić, M., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2018). Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. in Food Chemistry
Elsevier Sci Ltd, Oxford., 269, 43-52.
https://doi.org/10.1016/j.foodchem.2018.06.138

Minić SL, Radomirović MŽ, Savković N, Radibratović M, Mihailović-Vesić J, Vasović T, Nikolić M, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. in Food Chemistry. 2018;269:43-52.
doi:10.1016/j.foodchem.2018.06.138 .

Minić, Simeon L., Radomirović, Mirjana Ž., Savković, Nina, Radibratović, Milica, Mihailović-Vesić, Jelena, Vasović, Tamara, Nikolić, Milan, Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions" in Food Chemistry, 269 (2018):43-52,
https://doi.org/10.1016/j.foodchem.2018.06.138 . .

TY  - DATA
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Savković, Nina
AU  - Radibratović, Milica
AU  - Mihailović-Vesić, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3187
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3187
ER  - 

@misc{
author = "Minić, Simeon L. and Radomirović, Mirjana Ž. and Savković, Nina and Radibratović, Milica and Mihailović-Vesić, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3187"
}

Minić, S. L., Radomirović, M. Ž., Savković, N., Radibratović, M., Mihailović-Vesić, J., Vasović, T., Nikolić, M., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2018). Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138. in Food Chemistry
Elsevier Sci Ltd, Oxford..
https://hdl.handle.net/21.15107/rcub_cherry_3187

Minić SL, Radomirović MŽ, Savković N, Radibratović M, Mihailović-Vesić J, Vasović T, Nikolić M, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138. in Food Chemistry. 2018;.
https://hdl.handle.net/21.15107/rcub_cherry_3187 .

Minić, Simeon L., Radomirović, Mirjana Ž., Savković, Nina, Radibratović, Milica, Mihailović-Vesić, Jelena, Vasović, Tamara, Nikolić, Milan, Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138" in Food Chemistry (2018),
https://hdl.handle.net/21.15107/rcub_cherry_3187 .

TY  - DATA
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3225
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3225
ER  - 

@misc{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3225"
}

Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T.. (2018). Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113. in Clinical and Experimental Allergy
Wiley, Hoboken..
https://hdl.handle.net/21.15107/rcub_cherry_3225

Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, Ćirković-Veličković T. Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113. in Clinical and Experimental Allergy. 2018;.
https://hdl.handle.net/21.15107/rcub_cherry_3225 .

Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Mihailović-Vesić, Jelena, Radibratović, Milica, Radosavljević, Jelena, Burazer, Lidija M., Milčić, Miloš K., Smiljanić, Katarina, van Hage, Marianne, Ćirković-Veličković, Tanja, "Supplementary data for the article: Prodic, I.; Stanic-Vucinic, D.; Apostolovic, D.; Mihailovic, J.; Radibratovic, M.; Radosavljevic, J.; Burazer, L.; Milcic, M.; Smiljanic, K.; van Hage, M.; et al. Influence of Peanut Matrix on Stability of Allergens in Gastric-Simulated Digesta: 2S Albumins Are Main Contributors to the IgE Reactivity of Short Digestion-Resistant Peptides. Clinical and Experimental Allergy 2018, 48 (6), 731–740. https://doi.org/10.1111/cea.13113" in Clinical and Experimental Allergy (2018),
https://hdl.handle.net/21.15107/rcub_cherry_3225 .

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Savković, Nina
AU  - Radibratović, Milica
AU  - Mihailović-Vesić, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2197
AB  - In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions
VL  - 269
SP  - 43
EP  - 52
DO  - 10.1016/j.foodchem.2018.06.138
ER  - 

@article{
author = "Minić, Simeon L. and Radomirović, Mirjana Ž. and Savković, Nina and Radibratović, Milica and Mihailović-Vesić, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions",
volume = "269",
pages = "43-52",
doi = "10.1016/j.foodchem.2018.06.138"
}

Minić, S. L., Radomirović, M. Ž., Savković, N., Radibratović, M., Mihailović-Vesić, J., Vasović, T., Nikolić, M., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2018). Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. in Food Chemistry
Elsevier Sci Ltd, Oxford., 269, 43-52.
https://doi.org/10.1016/j.foodchem.2018.06.138

Minić SL, Radomirović MŽ, Savković N, Radibratović M, Mihailović-Vesić J, Vasović T, Nikolić M, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. in Food Chemistry. 2018;269:43-52.
doi:10.1016/j.foodchem.2018.06.138 .

Minić, Simeon L., Radomirović, Mirjana Ž., Savković, Nina, Radibratović, Milica, Mihailović-Vesić, Jelena, Vasović, Tamara, Nikolić, Milan, Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions" in Food Chemistry, 269 (2018):43-52,
https://doi.org/10.1016/j.foodchem.2018.06.138 . .

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3224
AB  - BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
VL  - 48
IS  - 6
SP  - 731
EP  - 740
DO  - 10.1111/cea.13113
ER  - 

@article{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
volume = "48",
number = "6",
pages = "731-740",
doi = "10.1111/cea.13113"
}

Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T.. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy
Wiley, Hoboken., 48(6), 731-740.
https://doi.org/10.1111/cea.13113

Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, Ćirković-Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy. 2018;48(6):731-740.
doi:10.1111/cea.13113 .

Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Mihailović-Vesić, Jelena, Radibratović, Milica, Radosavljević, Jelena, Burazer, Lidija M., Milčić, Miloš K., Smiljanić, Katarina, van Hage, Marianne, Ćirković-Veličković, Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" in Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 . .

TY  - JOUR
AU  - Prodić, Ivana
AU  - Stanić-Vučinić, Dragana
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Radibratović, Milica
AU  - Radosavljević, Jelena
AU  - Burazer, Lidija M.
AU  - Milčić, Miloš K.
AU  - Smiljanić, Katarina
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2155
AB  - BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.
PB  - Wiley, Hoboken
T2  - Clinical and Experimental Allergy
T1  - Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides
VL  - 48
IS  - 6
SP  - 731
EP  - 740
DO  - 10.1111/cea.13113
ER  - 

@article{
author = "Prodić, Ivana and Stanić-Vučinić, Dragana and Apostolović, Danijela and Mihailović-Vesić, Jelena and Radibratović, Milica and Radosavljević, Jelena and Burazer, Lidija M. and Milčić, Miloš K. and Smiljanić, Katarina and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "BackgroundMost food allergens sensitizing via the gastrointestinal tract are stable proteins that are resistant to pepsin digestion, in particular major peanut allergens, Ara h 2 and Ara h 6. Survival of their large fragments is essential for sensitizing capacity. However, the immunoreactive proteins/peptides to which the immune system of the gastrointestinal tract is exposed during digestion of peanut proteins are unknown. Particularly, the IgE reactivity of short digestion-resistant peptides (SDRPs;  lt 10kDa) released by gastric digestion under standardized and physiologically relevant invitro conditions has not been investigated. ObjectiveThe aim of this study was to investigate and identify digestion products of major peanut allergens and in particular to examine IgE reactivity of SDRPs released by pepsin digestion of whole peanut grains. MethodsTwo-dimensional gel-based proteomics and shotgun peptidomics, immunoblotting with allergen-specific antibodies from peanut-sensitized patients, enzyme-linked immunosorbent inhibition assay and ImmunoCAP tests, including far ultraviolet-circular dichroism spectroscopy were used to identify and characterize peanut digesta. ResultsAra h 2 and Ara h 6 remained mostly intact, and SDRPs from Ara h 2 were more potent in inhibiting IgE binding than Ara h 1 and Ara 3. Ara h 1 and Ara h 3 exhibited sequential digestion into a series of digestion-resistant peptides with preserved allergenic capacity. A high number of identified SDRPs from Ara h 1, Ara h 2 and Ara h 3 were part of short continuous epitope sequences and possessed substantial allergenic potential. Conclusion and Clinical RelevancePeanut grain digestion by oral and gastric phase enzymes generates mixture of products, where the major peanut allergens remain intact and their digested peptides have preserved allergenic capacity highlighting their important roles in allergic reactions to peanut.",
publisher = "Wiley, Hoboken",
journal = "Clinical and Experimental Allergy",
title = "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides",
volume = "48",
number = "6",
pages = "731-740",
doi = "10.1111/cea.13113"
}

Prodić, I., Stanić-Vučinić, D., Apostolović, D., Mihailović-Vesić, J., Radibratović, M., Radosavljević, J., Burazer, L. M., Milčić, M. K., Smiljanić, K., van Hage, M.,& Ćirković-Veličković, T.. (2018). Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy
Wiley, Hoboken., 48(6), 731-740.
https://doi.org/10.1111/cea.13113

Prodić I, Stanić-Vučinić D, Apostolović D, Mihailović-Vesić J, Radibratović M, Radosavljević J, Burazer LM, Milčić MK, Smiljanić K, van Hage M, Ćirković-Veličković T. Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides. in Clinical and Experimental Allergy. 2018;48(6):731-740.
doi:10.1111/cea.13113 .

Prodić, Ivana, Stanić-Vučinić, Dragana, Apostolović, Danijela, Mihailović-Vesić, Jelena, Radibratović, Milica, Radosavljević, Jelena, Burazer, Lidija M., Milčić, Miloš K., Smiljanić, Katarina, van Hage, Marianne, Ćirković-Veličković, Tanja, "Influence of peanut matrix on stability of allergens in gastric-simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion-resistant peptides" in Clinical and Experimental Allergy, 48, no. 6 (2018):731-740,
https://doi.org/10.1111/cea.13113 . .

TY  - CONF
AU  - Radosavljević, Jelena
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Atanasković-Marković, Marina
AU  - Burazer, Lidija M.
AU  - van Hage, Marianne
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2176
PB  - Wiley, Hoboken
C3  - FEBS OPEN BIO
T1  - Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes
VL  - 8
SP  - 257
EP  - 257
UR  - https://hdl.handle.net/21.15107/rcub_cherry_2176
ER  - 

@conference{
author = "Radosavljević, Jelena and Apostolović, Danijela and Mihailović-Vesić, Jelena and Atanasković-Marković, Marina and Burazer, Lidija M. and van Hage, Marianne and Ćirković-Veličković, Tanja",
year = "2018",
publisher = "Wiley, Hoboken",
journal = "FEBS OPEN BIO",
title = "Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes",
volume = "8",
pages = "257-257",
url = "https://hdl.handle.net/21.15107/rcub_cherry_2176"
}

Radosavljević, J., Apostolović, D., Mihailović-Vesić, J., Atanasković-Marković, M., Burazer, L. M., van Hage, M.,& Ćirković-Veličković, T.. (2018). Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes. in FEBS OPEN BIO
Wiley, Hoboken., 8, 257-257.
https://hdl.handle.net/21.15107/rcub_cherry_2176

Radosavljević J, Apostolović D, Mihailović-Vesić J, Atanasković-Marković M, Burazer LM, van Hage M, Ćirković-Veličković T. Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes. in FEBS OPEN BIO. 2018;8:257-257.
https://hdl.handle.net/21.15107/rcub_cherry_2176 .

Radosavljević, Jelena, Apostolović, Danijela, Mihailović-Vesić, Jelena, Atanasković-Marković, Marina, Burazer, Lidija M., van Hage, Marianne, Ćirković-Veličković, Tanja, "Digestomics of cow's milk: casein-derived digestion-resistant peptides aggregate into functional complexes" in FEBS OPEN BIO, 8 (2018):257-257,
https://hdl.handle.net/21.15107/rcub_cherry_2176 .

TY  - DATA
AU  - Apostolović, Danijela
AU  - Krstić-Ristivojević, Maja
AU  - Mihailović-Vesić, Jelena
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3020
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Supplementary data for article: Apostolovic, D.; Krstic, M.; Mihailovic, J.; Starkhammar, M.; Cirkovic Velickovic, T.; Hamsten, C.; Van Hage, M. Peptidomics of an in Vitro Digested α-Gal Carrying Protein Revealed IgE-Reactive Peptides. Scientific Reports 2017, 7 (1). https://doi.org/10.1038/s41598-017-05355-4
VL  - 7
IS  - 1
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3020
ER  - 

@misc{
author = "Apostolović, Danijela and Krstić-Ristivojević, Maja and Mihailović-Vesić, Jelena and Starkhammar, Maria and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2017",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Supplementary data for article: Apostolovic, D.; Krstic, M.; Mihailovic, J.; Starkhammar, M.; Cirkovic Velickovic, T.; Hamsten, C.; Van Hage, M. Peptidomics of an in Vitro Digested α-Gal Carrying Protein Revealed IgE-Reactive Peptides. Scientific Reports 2017, 7 (1). https://doi.org/10.1038/s41598-017-05355-4",
volume = "7",
number = "1",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3020"
}

Apostolović, D., Krstić-Ristivojević, M., Mihailović-Vesić, J., Starkhammar, M., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M.. (2017). Supplementary data for article: Apostolovic, D.; Krstic, M.; Mihailovic, J.; Starkhammar, M.; Cirkovic Velickovic, T.; Hamsten, C.; Van Hage, M. Peptidomics of an in Vitro Digested α-Gal Carrying Protein Revealed IgE-Reactive Peptides. Scientific Reports 2017, 7 (1). https://doi.org/10.1038/s41598-017-05355-4. in Scientific Reports
Nature Publishing Group, London., 7(1).
https://hdl.handle.net/21.15107/rcub_cherry_3020

Apostolović D, Krstić-Ristivojević M, Mihailović-Vesić J, Starkhammar M, Ćirković-Veličković T, Hamsten C, van Hage M. Supplementary data for article: Apostolovic, D.; Krstic, M.; Mihailovic, J.; Starkhammar, M.; Cirkovic Velickovic, T.; Hamsten, C.; Van Hage, M. Peptidomics of an in Vitro Digested α-Gal Carrying Protein Revealed IgE-Reactive Peptides. Scientific Reports 2017, 7 (1). https://doi.org/10.1038/s41598-017-05355-4. in Scientific Reports. 2017;7(1).
https://hdl.handle.net/21.15107/rcub_cherry_3020 .

Apostolović, Danijela, Krstić-Ristivojević, Maja, Mihailović-Vesić, Jelena, Starkhammar, Maria, Ćirković-Veličković, Tanja, Hamsten, Carl, van Hage, Marianne, "Supplementary data for article: Apostolovic, D.; Krstic, M.; Mihailovic, J.; Starkhammar, M.; Cirkovic Velickovic, T.; Hamsten, C.; Van Hage, M. Peptidomics of an in Vitro Digested α-Gal Carrying Protein Revealed IgE-Reactive Peptides. Scientific Reports 2017, 7 (1). https://doi.org/10.1038/s41598-017-05355-4" in Scientific Reports, 7, no. 1 (2017),
https://hdl.handle.net/21.15107/rcub_cherry_3020 .

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Krstić-Ristivojević, Maja
AU  - Mihailović-Vesić, Jelena
AU  - Starkhammar, Maria
AU  - Ćirković-Veličković, Tanja
AU  - Hamsten, Carl
AU  - van Hage, Marianne
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2486
AB  - The mammalian carbohydrate galactose-alpha 1,3-galactose (alpha-Gal) causes a novel form of food allergy, red meat allergy, where patients experience severe allergic reactions several hours after red meat consumption. Here we explored gastric digestion of alpha-Gal glycoproteins using an in vitro model. Bovine thyroglobulin (BTG), a typical alpha-Gal carrying glycoprotein, was digested with pepsin. The resulting peptides were characterised by SDS PAGE, immunoblot and ImmunoCAP using sera from 20 red meat allergic patients. During pepsinolysis of BTG, a wide range of peptide bands was observed of which 14 to 17 kDa peptides remained stable throughout the gastric phase. The presence of the alpha-Gal epitope on the obtained peptides was demonstrated by an anti-alpha-Gal antibody and IgE from red meat allergic patients. The alpha-Gal digests were able to inhibit up to 86% of IgE reactivity to BTG. Importantly, basophil activation test demonstrated that the allergenic activity of BTG was retained after digestion in all four tested patients. Mass spectrometry-based peptidomics revealed that these peptides represent mostly internal and C-terminal parts of the protein, where the most potent IgE-binding alpha-Gal residues were identified at Asn(1756), Asn(1850) and Asn(2231). Thus allergenic a-Gal epitopes are stable to pepsinolysis, reinforcing their role as clinically relevant food allergens.
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Peptidomics of an in vitro digested alpha-Gal carrying protein revealed IgE-reactive peptides
VL  - 7
DO  - 10.1038/s41598-017-05355-4
ER  - 

@article{
author = "Apostolović, Danijela and Krstić-Ristivojević, Maja and Mihailović-Vesić, Jelena and Starkhammar, Maria and Ćirković-Veličković, Tanja and Hamsten, Carl and van Hage, Marianne",
year = "2017",
abstract = "The mammalian carbohydrate galactose-alpha 1,3-galactose (alpha-Gal) causes a novel form of food allergy, red meat allergy, where patients experience severe allergic reactions several hours after red meat consumption. Here we explored gastric digestion of alpha-Gal glycoproteins using an in vitro model. Bovine thyroglobulin (BTG), a typical alpha-Gal carrying glycoprotein, was digested with pepsin. The resulting peptides were characterised by SDS PAGE, immunoblot and ImmunoCAP using sera from 20 red meat allergic patients. During pepsinolysis of BTG, a wide range of peptide bands was observed of which 14 to 17 kDa peptides remained stable throughout the gastric phase. The presence of the alpha-Gal epitope on the obtained peptides was demonstrated by an anti-alpha-Gal antibody and IgE from red meat allergic patients. The alpha-Gal digests were able to inhibit up to 86% of IgE reactivity to BTG. Importantly, basophil activation test demonstrated that the allergenic activity of BTG was retained after digestion in all four tested patients. Mass spectrometry-based peptidomics revealed that these peptides represent mostly internal and C-terminal parts of the protein, where the most potent IgE-binding alpha-Gal residues were identified at Asn(1756), Asn(1850) and Asn(2231). Thus allergenic a-Gal epitopes are stable to pepsinolysis, reinforcing their role as clinically relevant food allergens.",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Peptidomics of an in vitro digested alpha-Gal carrying protein revealed IgE-reactive peptides",
volume = "7",
doi = "10.1038/s41598-017-05355-4"
}

Apostolović, D., Krstić-Ristivojević, M., Mihailović-Vesić, J., Starkhammar, M., Ćirković-Veličković, T., Hamsten, C.,& van Hage, M.. (2017). Peptidomics of an in vitro digested alpha-Gal carrying protein revealed IgE-reactive peptides. in Scientific Reports
Nature Publishing Group, London., 7.
https://doi.org/10.1038/s41598-017-05355-4

Apostolović D, Krstić-Ristivojević M, Mihailović-Vesić J, Starkhammar M, Ćirković-Veličković T, Hamsten C, van Hage M. Peptidomics of an in vitro digested alpha-Gal carrying protein revealed IgE-reactive peptides. in Scientific Reports. 2017;7.
doi:10.1038/s41598-017-05355-4 .

Apostolović, Danijela, Krstić-Ristivojević, Maja, Mihailović-Vesić, Jelena, Starkhammar, Maria, Ćirković-Veličković, Tanja, Hamsten, Carl, van Hage, Marianne, "Peptidomics of an in vitro digested alpha-Gal carrying protein revealed IgE-reactive peptides" in Scientific Reports, 7 (2017),
https://doi.org/10.1038/s41598-017-05355-4 . .

TY  - JOUR
AU  - Peruško, Marija
AU  - Al-Hanish, Ayah
AU  - Mihailović-Vesić, Jelena
AU  - Minić, Simeon L.
AU  - Trifunović, Sara
AU  - Prodić, Ivana
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2456
AB  - Major green tea catechin, epigallocatechin-3-gallate (EGCG), binds non-covalently to numerous dietary proteins, including beta-lactoglobulin of cow's milk. The effects of glycation of proteins via Maillard reaction on the binding capacity for polyphenols and the antiradical properties of the formed complexes have not been studied previously. Binding constant of BLG glycated by milk sugar lactose to EGCG was measured by the method of fluorophore quenching. Binding of EGCG was confirmed by CD and FTIR. The antioxidative properties of the complexes were examined by measuring ABTS radical scavenging capacity, superoxide anion scavenging capacity and total reducing power assay. Glycation of BLG does not significantly influence the binding constant of EGCG for the protein. Conformational changes were observed for both native and glycated BLG upon complexation with EGCG. Masking effect of polyphenol complexation on the antioxidative potential of the protein was of the similar degree for both glycated BLG and native BLG. (C) 2017 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction
VL  - 232
SP  - 744
EP  - 752
DO  - 10.1016/j.foodchem.2017.04.074
ER  - 

@article{
author = "Peruško, Marija and Al-Hanish, Ayah and Mihailović-Vesić, Jelena and Minić, Simeon L. and Trifunović, Sara and Prodić, Ivana and Ćirković-Veličković, Tanja",
year = "2017",
abstract = "Major green tea catechin, epigallocatechin-3-gallate (EGCG), binds non-covalently to numerous dietary proteins, including beta-lactoglobulin of cow's milk. The effects of glycation of proteins via Maillard reaction on the binding capacity for polyphenols and the antiradical properties of the formed complexes have not been studied previously. Binding constant of BLG glycated by milk sugar lactose to EGCG was measured by the method of fluorophore quenching. Binding of EGCG was confirmed by CD and FTIR. The antioxidative properties of the complexes were examined by measuring ABTS radical scavenging capacity, superoxide anion scavenging capacity and total reducing power assay. Glycation of BLG does not significantly influence the binding constant of EGCG for the protein. Conformational changes were observed for both native and glycated BLG upon complexation with EGCG. Masking effect of polyphenol complexation on the antioxidative potential of the protein was of the similar degree for both glycated BLG and native BLG. (C) 2017 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction",
volume = "232",
pages = "744-752",
doi = "10.1016/j.foodchem.2017.04.074"
}

Peruško, M., Al-Hanish, A., Mihailović-Vesić, J., Minić, S. L., Trifunović, S., Prodić, I.,& Ćirković-Veličković, T.. (2017). Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction. in Food Chemistry
Elsevier Sci Ltd, Oxford., 232, 744-752.
https://doi.org/10.1016/j.foodchem.2017.04.074

Peruško M, Al-Hanish A, Mihailović-Vesić J, Minić SL, Trifunović S, Prodić I, Ćirković-Veličković T. Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction. in Food Chemistry. 2017;232:744-752.
doi:10.1016/j.foodchem.2017.04.074 .

Peruško, Marija, Al-Hanish, Ayah, Mihailović-Vesić, Jelena, Minić, Simeon L., Trifunović, Sara, Prodić, Ivana, Ćirković-Veličković, Tanja, "Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction" in Food Chemistry, 232 (2017):744-752,
https://doi.org/10.1016/j.foodchem.2017.04.074 . .

TY  - DATA
AU  - Peruško, Marija
AU  - Al-Hanish, Ayah
AU  - Mihailović-Vesić, Jelena
AU  - Minić, Simeon L.
AU  - Trifunović, Sara
AU  - Prodić, Ivana
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3027
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Supplementary data for article: Peruško, M.; Al-Hanish, A.; Mihailović-Vesić, J.; Minić, S. L.; Trifunović, S.; Prodić, I.; Ćirković-Veličković, T. Antioxidative Capacity and Binding Affinity of the Complex of Green Tea Catechin and Beta-Lactoglobulin Glycated by the Maillard Reaction. Food Chemistry 2017, 232, 744–752. https://doi.org/10.1016/j.foodchem.2017.04.074
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3027
ER  - 

@misc{
author = "Peruško, Marija and Al-Hanish, Ayah and Mihailović-Vesić, Jelena and Minić, Simeon L. and Trifunović, Sara and Prodić, Ivana and Ćirković-Veličković, Tanja",
year = "2017",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Supplementary data for article: Peruško, M.; Al-Hanish, A.; Mihailović-Vesić, J.; Minić, S. L.; Trifunović, S.; Prodić, I.; Ćirković-Veličković, T. Antioxidative Capacity and Binding Affinity of the Complex of Green Tea Catechin and Beta-Lactoglobulin Glycated by the Maillard Reaction. Food Chemistry 2017, 232, 744–752. https://doi.org/10.1016/j.foodchem.2017.04.074",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3027"
}

Peruško, M., Al-Hanish, A., Mihailović-Vesić, J., Minić, S. L., Trifunović, S., Prodić, I.,& Ćirković-Veličković, T.. (2017). Supplementary data for article: Peruško, M.; Al-Hanish, A.; Mihailović-Vesić, J.; Minić, S. L.; Trifunović, S.; Prodić, I.; Ćirković-Veličković, T. Antioxidative Capacity and Binding Affinity of the Complex of Green Tea Catechin and Beta-Lactoglobulin Glycated by the Maillard Reaction. Food Chemistry 2017, 232, 744–752. https://doi.org/10.1016/j.foodchem.2017.04.074. in Food Chemistry
Elsevier Sci Ltd, Oxford..
https://hdl.handle.net/21.15107/rcub_cherry_3027

Peruško M, Al-Hanish A, Mihailović-Vesić J, Minić SL, Trifunović S, Prodić I, Ćirković-Veličković T. Supplementary data for article: Peruško, M.; Al-Hanish, A.; Mihailović-Vesić, J.; Minić, S. L.; Trifunović, S.; Prodić, I.; Ćirković-Veličković, T. Antioxidative Capacity and Binding Affinity of the Complex of Green Tea Catechin and Beta-Lactoglobulin Glycated by the Maillard Reaction. Food Chemistry 2017, 232, 744–752. https://doi.org/10.1016/j.foodchem.2017.04.074. in Food Chemistry. 2017;.
https://hdl.handle.net/21.15107/rcub_cherry_3027 .

Peruško, Marija, Al-Hanish, Ayah, Mihailović-Vesić, Jelena, Minić, Simeon L., Trifunović, Sara, Prodić, Ivana, Ćirković-Veličković, Tanja, "Supplementary data for article: Peruško, M.; Al-Hanish, A.; Mihailović-Vesić, J.; Minić, S. L.; Trifunović, S.; Prodić, I.; Ćirković-Veličković, T. Antioxidative Capacity and Binding Affinity of the Complex of Green Tea Catechin and Beta-Lactoglobulin Glycated by the Maillard Reaction. Food Chemistry 2017, 232, 744–752. https://doi.org/10.1016/j.foodchem.2017.04.074" in Food Chemistry (2017),
https://hdl.handle.net/21.15107/rcub_cherry_3027 .

TY  - CONF
AU  - Stein, Elisabeth
AU  - Mihailović-Vesić, Jelena
AU  - Inić-Kanada, Aleksandra
AU  - Smiljanić, Katarina
AU  - Peruško, Marija
AU  - Trifunović, Sara
AU  - Schuerer, Nadine
AU  - Stanić-Vučinić, Dragana
AU  - Ghasemian, Ehsan
AU  - Barisani-Asenbauer, Talin
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2139
PB  - Assoc Research Vision Ophthalmology Inc, Rockville
C3  - Investigative Ophthalmology and Visual Science
T1  - Quantitative proteome study of Chlamydia trachomatis ocular serovar B proteins associated with trachomatous trichiasis
VL  - 58
IS  - 8
UR  - https://hdl.handle.net/21.15107/rcub_cherry_2139
ER  - 

@conference{
author = "Stein, Elisabeth and Mihailović-Vesić, Jelena and Inić-Kanada, Aleksandra and Smiljanić, Katarina and Peruško, Marija and Trifunović, Sara and Schuerer, Nadine and Stanić-Vučinić, Dragana and Ghasemian, Ehsan and Barisani-Asenbauer, Talin and Ćirković-Veličković, Tanja",
year = "2017",
publisher = "Assoc Research Vision Ophthalmology Inc, Rockville",
journal = "Investigative Ophthalmology and Visual Science",
title = "Quantitative proteome study of Chlamydia trachomatis ocular serovar B proteins associated with trachomatous trichiasis",
volume = "58",
number = "8",
url = "https://hdl.handle.net/21.15107/rcub_cherry_2139"
}

Stein, E., Mihailović-Vesić, J., Inić-Kanada, A., Smiljanić, K., Peruško, M., Trifunović, S., Schuerer, N., Stanić-Vučinić, D., Ghasemian, E., Barisani-Asenbauer, T.,& Ćirković-Veličković, T.. (2017). Quantitative proteome study of Chlamydia trachomatis ocular serovar B proteins associated with trachomatous trichiasis. in Investigative Ophthalmology and Visual Science
Assoc Research Vision Ophthalmology Inc, Rockville., 58(8).
https://hdl.handle.net/21.15107/rcub_cherry_2139

Stein E, Mihailović-Vesić J, Inić-Kanada A, Smiljanić K, Peruško M, Trifunović S, Schuerer N, Stanić-Vučinić D, Ghasemian E, Barisani-Asenbauer T, Ćirković-Veličković T. Quantitative proteome study of Chlamydia trachomatis ocular serovar B proteins associated with trachomatous trichiasis. in Investigative Ophthalmology and Visual Science. 2017;58(8).
https://hdl.handle.net/21.15107/rcub_cherry_2139 .

Stein, Elisabeth, Mihailović-Vesić, Jelena, Inić-Kanada, Aleksandra, Smiljanić, Katarina, Peruško, Marija, Trifunović, Sara, Schuerer, Nadine, Stanić-Vučinić, Dragana, Ghasemian, Ehsan, Barisani-Asenbauer, Talin, Ćirković-Veličković, Tanja, "Quantitative proteome study of Chlamydia trachomatis ocular serovar B proteins associated with trachomatous trichiasis" in Investigative Ophthalmology and Visual Science, 58, no. 8 (2017),
https://hdl.handle.net/21.15107/rcub_cherry_2139 .

TY  - DATA
AU  - Apostolović, Danijela
AU  - Stanić-Vučinić, Dragana
AU  - de Jongh, Harmen H. J.
AU  - de Jong, Govardus A. H.
AU  - Mihailović-Vesić, Jelena
AU  - Radosavljević, Jelena
AU  - Radibratović, Milica
AU  - Nordlee, Julie A.
AU  - Baumert, Joseph L.
AU  - Milčić, Miloš K.
AU  - Taylor, Steve L.
AU  - Clua, Nuria Garrido
AU  - Ćirković-Veličković, Tanja
AU  - Koppelman, Stef J.
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3415
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3415
ER  - 

@misc{
author = "Apostolović, Danijela and Stanić-Vučinić, Dragana and de Jongh, Harmen H. J. and de Jong, Govardus A. H. and Mihailović-Vesić, Jelena and Radosavljević, Jelena and Radibratović, Milica and Nordlee, Julie A. and Baumert, Joseph L. and Milčić, Miloš K. and Taylor, Steve L. and Clua, Nuria Garrido and Ćirković-Veličković, Tanja and Koppelman, Stef J.",
year = "2016",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3415"
}

Apostolović, D., Stanić-Vučinić, D., de Jongh, H. H. J., de Jong, G. A. H., Mihailović-Vesić, J., Radosavljević, J., Radibratović, M., Nordlee, J. A., Baumert, J. L., Milčić, M. K., Taylor, S. L., Clua, N. G., Ćirković-Veličković, T.,& Koppelman, S. J.. (2016). Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249. in Scientific Reports
Nature Publishing Group, London..
https://hdl.handle.net/21.15107/rcub_cherry_3415

Apostolović D, Stanić-Vučinić D, de Jongh HHJ, de Jong GAH, Mihailović-Vesić J, Radosavljević J, Radibratović M, Nordlee JA, Baumert JL, Milčić MK, Taylor SL, Clua NG, Ćirković-Veličković T, Koppelman SJ. Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249. in Scientific Reports. 2016;.
https://hdl.handle.net/21.15107/rcub_cherry_3415 .

Apostolović, Danijela, Stanić-Vučinić, Dragana, de Jongh, Harmen H. J., de Jong, Govardus A. H., Mihailović-Vesić, Jelena, Radosavljević, Jelena, Radibratović, Milica, Nordlee, Julie A., Baumert, Joseph L., Milčić, Miloš K., Taylor, Steve L., Clua, Nuria Garrido, Ćirković-Veličković, Tanja, Koppelman, Stef J., "Supplementary data for the article: Apostolovic, D.; Stanic-Vucinic, D.; De Jongh, H. H. J.; De Jong, G. A. H.; Mihailovic, J.; Radosavljevic, J.; Radibratovic, M.; Nordlee, J. A.; Baumert, J. L.; Milcic, M.; et al. Conformational Stability of Digestion-Resistant Peptides of Peanut Conglutins Reveals the Molecular Basis of Their Allergenicity. Scientific Reports 2016, 6. https://doi.org/10.1038/srep29249" in Scientific Reports (2016),
https://hdl.handle.net/21.15107/rcub_cherry_3415 .

TY  - DATA
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  - https://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
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3585
ER  - 

@misc{
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",
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",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3585"
}

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. in Food Hydrocolloids
Elsevier Sci Ltd, Oxford..
https://hdl.handle.net/21.15107/rcub_cherry_3585

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. in Food Hydrocolloids. 2016;.
https://hdl.handle.net/21.15107/rcub_cherry_3585 .

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" in Food Hydrocolloids (2016),
https://hdl.handle.net/21.15107/rcub_cherry_3585 .

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Mihailović-Vesić, Jelena
AU  - Krstić-Ristivojević, Maja
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3444
AB  - C-phycocyanin, the major protein of cyanobacteria Spirulina, possesses significant antioxidant, anti-cancer, anti-inflammatory and immunomodulatory effects, ascribed to covalently attached linear tetrapyrrole chromophore phycocyanobilin. There are no literature data about structure and biological activities of released peptides with bound chromophore in C-phycocyanin digest. This study aims to identify chromopeptides obtained after pepsin digestion of C-phycocyanin and to examine their bioactivities. C-phycocyanin is rapidly digested by pepsin in simulated gastric fluid. The structure of released chromopeptides was analyzed by high resolution tandem mass spectrometry and peptides varying in size from 2 to 13 amino acid residues were identified in both subunits of C-phycocyanin. Following separation by HPLC, chromopeptides were analyzed for potential bioactivities. It was shown that all five chromopeptide fractions have significant antioxidant and metal-chelating activities and show cytotoxic effect on human cervical adenocarcinoma and epithelial colonic cancer cell lines. In addition, chromopeptides protect human erythrocytes from free radical-induced hemolysis in antioxidative capacity dependant manner. There was a positive correlation between antioxidative potency and other biological activities of chromopeptides. Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin whose activity is mostly related to the antioxidative potency provided by chromophore. (C) 2016 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Proteomics
T1  - Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin, a blue-colored biliprotein of microalga Spirulina
VL  - 147
SP  - 132
EP  - 139
DO  - 10.1016/j.jprot.2016.03.043
ER  - 

@article{
author = "Minić, Simeon L. and Stanić-Vučinić, Dragana and Mihailović-Vesić, Jelena and Krstić-Ristivojević, Maja and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2016",
abstract = "C-phycocyanin, the major protein of cyanobacteria Spirulina, possesses significant antioxidant, anti-cancer, anti-inflammatory and immunomodulatory effects, ascribed to covalently attached linear tetrapyrrole chromophore phycocyanobilin. There are no literature data about structure and biological activities of released peptides with bound chromophore in C-phycocyanin digest. This study aims to identify chromopeptides obtained after pepsin digestion of C-phycocyanin and to examine their bioactivities. C-phycocyanin is rapidly digested by pepsin in simulated gastric fluid. The structure of released chromopeptides was analyzed by high resolution tandem mass spectrometry and peptides varying in size from 2 to 13 amino acid residues were identified in both subunits of C-phycocyanin. Following separation by HPLC, chromopeptides were analyzed for potential bioactivities. It was shown that all five chromopeptide fractions have significant antioxidant and metal-chelating activities and show cytotoxic effect on human cervical adenocarcinoma and epithelial colonic cancer cell lines. In addition, chromopeptides protect human erythrocytes from free radical-induced hemolysis in antioxidative capacity dependant manner. There was a positive correlation between antioxidative potency and other biological activities of chromopeptides. Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin whose activity is mostly related to the antioxidative potency provided by chromophore. (C) 2016 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Proteomics",
title = "Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin, a blue-colored biliprotein of microalga Spirulina",
volume = "147",
pages = "132-139",
doi = "10.1016/j.jprot.2016.03.043"
}

Minić, S. L., Stanić-Vučinić, D., Mihailović-Vesić, J., Krstić-Ristivojević, M., Nikolić, M.,& Ćirković-Veličković, T.. (2016). Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin, a blue-colored biliprotein of microalga Spirulina. in Journal of Proteomics
Elsevier Science Bv, Amsterdam., 147, 132-139.
https://doi.org/10.1016/j.jprot.2016.03.043

Minić SL, Stanić-Vučinić D, Mihailović-Vesić J, Krstić-Ristivojević M, Nikolić M, Ćirković-Veličković T. Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin, a blue-colored biliprotein of microalga Spirulina. in Journal of Proteomics. 2016;147:132-139.
doi:10.1016/j.jprot.2016.03.043 .

Minić, Simeon L., Stanić-Vučinić, Dragana, Mihailović-Vesić, Jelena, Krstić-Ristivojević, Maja, Nikolić, Milan, Ćirković-Veličković, Tanja, "Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin, a blue-colored biliprotein of microalga Spirulina" in Journal of Proteomics, 147 (2016):132-139,
https://doi.org/10.1016/j.jprot.2016.03.043 . .

TY  - DATA
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Mihailović-Vesić, Jelena
AU  - Krstić-Ristivojević, Maja
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3445
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Proteomics
T1  - Supplementary data for the article: Minic, S. L.; Stanic-Vucinic, D.; Mihailovic, J.; Krstic, M.; Nikolic, M. R.; Velickovic, T. C. Digestion by Pepsin Releases Biologically Active Chromopeptides from C-Phycocyanin, a Blue-Colored Biliprotein of Microalga Spirulina. J. Proteomics 2016, 147, 132–139. https://doi.org/10.1016/j.jprot.2016.03.043
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3445
ER  - 

@misc{
author = "Minić, Simeon L. and Stanić-Vučinić, Dragana and Mihailović-Vesić, Jelena and Krstić-Ristivojević, Maja and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2016",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Proteomics",
title = "Supplementary data for the article: Minic, S. L.; Stanic-Vucinic, D.; Mihailovic, J.; Krstic, M.; Nikolic, M. R.; Velickovic, T. C. Digestion by Pepsin Releases Biologically Active Chromopeptides from C-Phycocyanin, a Blue-Colored Biliprotein of Microalga Spirulina. J. Proteomics 2016, 147, 132–139. https://doi.org/10.1016/j.jprot.2016.03.043",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3445"
}

Minić, S. L., Stanić-Vučinić, D., Mihailović-Vesić, J., Krstić-Ristivojević, M., Nikolić, M.,& Ćirković-Veličković, T.. (2016). Supplementary data for the article: Minic, S. L.; Stanic-Vucinic, D.; Mihailovic, J.; Krstic, M.; Nikolic, M. R.; Velickovic, T. C. Digestion by Pepsin Releases Biologically Active Chromopeptides from C-Phycocyanin, a Blue-Colored Biliprotein of Microalga Spirulina. J. Proteomics 2016, 147, 132–139. https://doi.org/10.1016/j.jprot.2016.03.043. in Journal of Proteomics
Elsevier Science Bv, Amsterdam..
https://hdl.handle.net/21.15107/rcub_cherry_3445

Minić SL, Stanić-Vučinić D, Mihailović-Vesić J, Krstić-Ristivojević M, Nikolić M, Ćirković-Veličković T. Supplementary data for the article: Minic, S. L.; Stanic-Vucinic, D.; Mihailovic, J.; Krstic, M.; Nikolic, M. R.; Velickovic, T. C. Digestion by Pepsin Releases Biologically Active Chromopeptides from C-Phycocyanin, a Blue-Colored Biliprotein of Microalga Spirulina. J. Proteomics 2016, 147, 132–139. https://doi.org/10.1016/j.jprot.2016.03.043. in Journal of Proteomics. 2016;.
https://hdl.handle.net/21.15107/rcub_cherry_3445 .

Minić, Simeon L., Stanić-Vučinić, Dragana, Mihailović-Vesić, Jelena, Krstić-Ristivojević, Maja, Nikolić, Milan, Ćirković-Veličković, Tanja, "Supplementary data for the article: Minic, S. L.; Stanic-Vucinic, D.; Mihailovic, J.; Krstic, M.; Nikolic, M. R.; Velickovic, T. C. Digestion by Pepsin Releases Biologically Active Chromopeptides from C-Phycocyanin, a Blue-Colored Biliprotein of Microalga Spirulina. J. Proteomics 2016, 147, 132–139. https://doi.org/10.1016/j.jprot.2016.03.043" in Journal of Proteomics (2016),
https://hdl.handle.net/21.15107/rcub_cherry_3445 .

TY  - DATA
AU  - Mihailović-Vesić, Jelena
AU  - Inić-Kanada, Aleksandra
AU  - Smiljanić, Katarina
AU  - Stein, Elisabeth
AU  - Barisani-Asenbauer, T.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3563
T2  - EuPA Open Proteomics
T1  - Supplementary data for the article: Mihailovic, J.; Inic-Kanada, A.; Smiljanic, K.; Stein, E.; Barisani-Asenbauer, T.; Cirkovic Velickovic, T. Lysine Acetylation of Major Chlamydia Trachomatis Antigens. EuPA Open Proteomics 2016, 10, 63–69. https://doi.org/10.1016/j.euprot.2016.01.007
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3563
ER  - 

@misc{
author = "Mihailović-Vesić, Jelena and Inić-Kanada, Aleksandra and Smiljanić, Katarina and Stein, Elisabeth and Barisani-Asenbauer, T. and Ćirković-Veličković, Tanja",
year = "2016",
journal = "EuPA Open Proteomics",
title = "Supplementary data for the article: Mihailovic, J.; Inic-Kanada, A.; Smiljanic, K.; Stein, E.; Barisani-Asenbauer, T.; Cirkovic Velickovic, T. Lysine Acetylation of Major Chlamydia Trachomatis Antigens. EuPA Open Proteomics 2016, 10, 63–69. https://doi.org/10.1016/j.euprot.2016.01.007",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3563"
}

Mihailović-Vesić, J., Inić-Kanada, A., Smiljanić, K., Stein, E., Barisani-Asenbauer, T.,& Ćirković-Veličković, T.. (2016). Supplementary data for the article: Mihailovic, J.; Inic-Kanada, A.; Smiljanic, K.; Stein, E.; Barisani-Asenbauer, T.; Cirkovic Velickovic, T. Lysine Acetylation of Major Chlamydia Trachomatis Antigens. EuPA Open Proteomics 2016, 10, 63–69. https://doi.org/10.1016/j.euprot.2016.01.007. in EuPA Open Proteomics.
https://hdl.handle.net/21.15107/rcub_cherry_3563

Mihailović-Vesić J, Inić-Kanada A, Smiljanić K, Stein E, Barisani-Asenbauer T, Ćirković-Veličković T. Supplementary data for the article: Mihailovic, J.; Inic-Kanada, A.; Smiljanic, K.; Stein, E.; Barisani-Asenbauer, T.; Cirkovic Velickovic, T. Lysine Acetylation of Major Chlamydia Trachomatis Antigens. EuPA Open Proteomics 2016, 10, 63–69. https://doi.org/10.1016/j.euprot.2016.01.007. in EuPA Open Proteomics. 2016;.
https://hdl.handle.net/21.15107/rcub_cherry_3563 .

Mihailović-Vesić, Jelena, Inić-Kanada, Aleksandra, Smiljanić, Katarina, Stein, Elisabeth, Barisani-Asenbauer, T., Ćirković-Veličković, Tanja, "Supplementary data for the article: Mihailovic, J.; Inic-Kanada, A.; Smiljanic, K.; Stein, E.; Barisani-Asenbauer, T.; Cirkovic Velickovic, T. Lysine Acetylation of Major Chlamydia Trachomatis Antigens. EuPA Open Proteomics 2016, 10, 63–69. https://doi.org/10.1016/j.euprot.2016.01.007" in EuPA Open Proteomics (2016),
https://hdl.handle.net/21.15107/rcub_cherry_3563 .

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Mihailović-Vesić, Jelena
AU  - Krstić-Ristivojević, Maja
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2313
AB  - C-phycocyanin, the major protein of cyanobacteria Spirulina, possesses significant antioxidant, anti-cancer, anti-inflammatory and immunomodulatory effects, ascribed to covalently attached linear tetrapyrrole chromophore phycocyanobilin. There are no literature data about structure and biological activities of released peptides with bound chromophore in C-phycocyanin digest. This study aims to identify chromopeptides obtained after pepsin digestion of C-phycocyanin and to examine their bioactivities. C-phycocyanin is rapidly digested by pepsin in simulated gastric fluid. The structure of released chromopeptides was analyzed by high resolution tandem mass spectrometry and peptides varying in size from 2 to 13 amino acid residues were identified in both subunits of C-phycocyanin. Following separation by HPLC, chromopeptides were analyzed for potential bioactivities. It was shown that all five chromopeptide fractions have significant antioxidant and metal-chelating activities and show cytotoxic effect on human cervical adenocarcinoma and epithelial colonic cancer cell lines. In addition, chromopeptides protect human erythrocytes from free radical-induced hemolysis in antioxidative capacity dependant manner. There was a positive correlation between antioxidative potency and other biological activities of chromopeptides. Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin whose activity is mostly related to the antioxidative potency provided by chromophore. (C) 2016 Elsevier B.V. All rights reserved.
PB  - Elsevier Science Bv, Amsterdam
T2  - Journal of Proteomics
T1  - Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin, a blue-colored biliprotein of microalga Spirulina
VL  - 147
SP  - 132
EP  - 139
DO  - 10.1016/j.jprot.2016.03.043
ER  - 

@article{
author = "Minić, Simeon L. and Stanić-Vučinić, Dragana and Mihailović-Vesić, Jelena and Krstić-Ristivojević, Maja and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2016",
abstract = "C-phycocyanin, the major protein of cyanobacteria Spirulina, possesses significant antioxidant, anti-cancer, anti-inflammatory and immunomodulatory effects, ascribed to covalently attached linear tetrapyrrole chromophore phycocyanobilin. There are no literature data about structure and biological activities of released peptides with bound chromophore in C-phycocyanin digest. This study aims to identify chromopeptides obtained after pepsin digestion of C-phycocyanin and to examine their bioactivities. C-phycocyanin is rapidly digested by pepsin in simulated gastric fluid. The structure of released chromopeptides was analyzed by high resolution tandem mass spectrometry and peptides varying in size from 2 to 13 amino acid residues were identified in both subunits of C-phycocyanin. Following separation by HPLC, chromopeptides were analyzed for potential bioactivities. It was shown that all five chromopeptide fractions have significant antioxidant and metal-chelating activities and show cytotoxic effect on human cervical adenocarcinoma and epithelial colonic cancer cell lines. In addition, chromopeptides protect human erythrocytes from free radical-induced hemolysis in antioxidative capacity dependant manner. There was a positive correlation between antioxidative potency and other biological activities of chromopeptides. Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin whose activity is mostly related to the antioxidative potency provided by chromophore. (C) 2016 Elsevier B.V. All rights reserved.",
publisher = "Elsevier Science Bv, Amsterdam",
journal = "Journal of Proteomics",
title = "Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin, a blue-colored biliprotein of microalga Spirulina",
volume = "147",
pages = "132-139",
doi = "10.1016/j.jprot.2016.03.043"
}

Minić, S. L., Stanić-Vučinić, D., Mihailović-Vesić, J., Krstić-Ristivojević, M., Nikolić, M.,& Ćirković-Veličković, T.. (2016). Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin, a blue-colored biliprotein of microalga Spirulina. in Journal of Proteomics
Elsevier Science Bv, Amsterdam., 147, 132-139.
https://doi.org/10.1016/j.jprot.2016.03.043

Minić SL, Stanić-Vučinić D, Mihailović-Vesić J, Krstić-Ristivojević M, Nikolić M, Ćirković-Veličković T. Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin, a blue-colored biliprotein of microalga Spirulina. in Journal of Proteomics. 2016;147:132-139.
doi:10.1016/j.jprot.2016.03.043 .

Minić, Simeon L., Stanić-Vučinić, Dragana, Mihailović-Vesić, Jelena, Krstić-Ristivojević, Maja, Nikolić, Milan, Ćirković-Veličković, Tanja, "Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin, a blue-colored biliprotein of microalga Spirulina" in Journal of Proteomics, 147 (2016):132-139,
https://doi.org/10.1016/j.jprot.2016.03.043 . .

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  - https://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",
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. in 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. in Food Hydrocolloids. 2016;61:241-250.
doi: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, "Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate" in Food Hydrocolloids, 61 (2016):241-250,
https://doi.org/10.1016/j.foodhyd.2016.05.012 . .

TY  - JOUR
AU  - Apostolović, Danijela
AU  - Stanić-Vučinić, Dragana
AU  - de Jongh, Harmen H. J.
AU  - de Jong, Govardus A. H.
AU  - Mihailović-Vesić, Jelena
AU  - Radosavljević, Jelena
AU  - Radibratović, Milica
AU  - Nordlee, Julie A.
AU  - Baumert, Joseph L.
AU  - Milčić, Miloš K.
AU  - Taylor, Steve L.
AU  - Clua, Nuria Garrido
AU  - Ćirković-Veličković, Tanja
AU  - Koppelman, Stef J.
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2273
AB  - Conglutins represent the major peanut allergens and are renowned for their resistance to gastrointestinal digestion. Our aim was to characterize the digestion-resistant peptides (DRPs) of conglutins by biochemical and biophysical methods followed by a molecular dynamics simulation in order to better understand the molecular basis of food protein allergenicity. We have mapped proteolysis sites at the N- and C-termini and at a limited internal segment, while other potential proteolysis sites remained unaffected. Molecular dynamics simulation showed that proteolysis only occurred in the vibrant regions of the proteins. DRPs appeared to be conformationally stable as intact conglutins. Also, the overall secondary structure and IgE-binding potency of DRPs was comparable to that of intact conglutins. The stability of conglutins toward gastro-intestinal digestion, combined with the conformational stability of the resulting DRPs provide conditions for optimal exposure to the intestinal immune system, providing an explanation for the extraordinary allergenicity of peanut conglutins.
PB  - Nature Publishing Group, London
T2  - Scientific Reports
T1  - Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity
VL  - 6
DO  - 10.1038/srep29249
ER  - 

@article{
author = "Apostolović, Danijela and Stanić-Vučinić, Dragana and de Jongh, Harmen H. J. and de Jong, Govardus A. H. and Mihailović-Vesić, Jelena and Radosavljević, Jelena and Radibratović, Milica and Nordlee, Julie A. and Baumert, Joseph L. and Milčić, Miloš K. and Taylor, Steve L. and Clua, Nuria Garrido and Ćirković-Veličković, Tanja and Koppelman, Stef J.",
year = "2016",
abstract = "Conglutins represent the major peanut allergens and are renowned for their resistance to gastrointestinal digestion. Our aim was to characterize the digestion-resistant peptides (DRPs) of conglutins by biochemical and biophysical methods followed by a molecular dynamics simulation in order to better understand the molecular basis of food protein allergenicity. We have mapped proteolysis sites at the N- and C-termini and at a limited internal segment, while other potential proteolysis sites remained unaffected. Molecular dynamics simulation showed that proteolysis only occurred in the vibrant regions of the proteins. DRPs appeared to be conformationally stable as intact conglutins. Also, the overall secondary structure and IgE-binding potency of DRPs was comparable to that of intact conglutins. The stability of conglutins toward gastro-intestinal digestion, combined with the conformational stability of the resulting DRPs provide conditions for optimal exposure to the intestinal immune system, providing an explanation for the extraordinary allergenicity of peanut conglutins.",
publisher = "Nature Publishing Group, London",
journal = "Scientific Reports",
title = "Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity",
volume = "6",
doi = "10.1038/srep29249"
}

Apostolović, D., Stanić-Vučinić, D., de Jongh, H. H. J., de Jong, G. A. H., Mihailović-Vesić, J., Radosavljević, J., Radibratović, M., Nordlee, J. A., Baumert, J. L., Milčić, M. K., Taylor, S. L., Clua, N. G., Ćirković-Veličković, T.,& Koppelman, S. J.. (2016). Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity. in Scientific Reports
Nature Publishing Group, London., 6.
https://doi.org/10.1038/srep29249

Apostolović D, Stanić-Vučinić D, de Jongh HHJ, de Jong GAH, Mihailović-Vesić J, Radosavljević J, Radibratović M, Nordlee JA, Baumert JL, Milčić MK, Taylor SL, Clua NG, Ćirković-Veličković T, Koppelman SJ. Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity. in Scientific Reports. 2016;6.
doi:10.1038/srep29249 .

Apostolović, Danijela, Stanić-Vučinić, Dragana, de Jongh, Harmen H. J., de Jong, Govardus A. H., Mihailović-Vesić, Jelena, Radosavljević, Jelena, Radibratović, Milica, Nordlee, Julie A., Baumert, Joseph L., Milčić, Miloš K., Taylor, Steve L., Clua, Nuria Garrido, Ćirković-Veličković, Tanja, Koppelman, Stef J., "Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity" in Scientific Reports, 6 (2016),
https://doi.org/10.1038/srep29249 . .

TY  - CONF
AU  - Barisani-Asenbauer, Talin
AU  - Inić-Kanada, Aleksandra
AU  - Smiljanić, Katarina
AU  - Stein, Elisabeth
AU  - Belaw, Yeshigeta
AU  - Elkheir, Balgesa
AU  - Mihailović-Vesić, Jelena
AU  - Chalabi, Hadeel
AU  - Schuerer, Nadine
AU  - Ghasemian, Ehsan
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2414
PB  - Assoc Research Vision Ophthalmology Inc, Rockville
C3  - Investigative Ophthalmology and Visual Science
T1  - Immunoproteomics of Relevant Chlamydial Antigens in Trachomatous Trichiasis Patients from Ethiopia and Sudan
VL  - 57
IS  - 12
UR  - https://hdl.handle.net/21.15107/rcub_cherry_2414
ER  - 

@conference{
author = "Barisani-Asenbauer, Talin and Inić-Kanada, Aleksandra and Smiljanić, Katarina and Stein, Elisabeth and Belaw, Yeshigeta and Elkheir, Balgesa and Mihailović-Vesić, Jelena and Chalabi, Hadeel and Schuerer, Nadine and Ghasemian, Ehsan and Ćirković-Veličković, Tanja",
year = "2016",
publisher = "Assoc Research Vision Ophthalmology Inc, Rockville",
journal = "Investigative Ophthalmology and Visual Science",
title = "Immunoproteomics of Relevant Chlamydial Antigens in Trachomatous Trichiasis Patients from Ethiopia and Sudan",
volume = "57",
number = "12",
url = "https://hdl.handle.net/21.15107/rcub_cherry_2414"
}

Barisani-Asenbauer, T., Inić-Kanada, A., Smiljanić, K., Stein, E., Belaw, Y., Elkheir, B., Mihailović-Vesić, J., Chalabi, H., Schuerer, N., Ghasemian, E.,& Ćirković-Veličković, T.. (2016). Immunoproteomics of Relevant Chlamydial Antigens in Trachomatous Trichiasis Patients from Ethiopia and Sudan. in Investigative Ophthalmology and Visual Science
Assoc Research Vision Ophthalmology Inc, Rockville., 57(12).
https://hdl.handle.net/21.15107/rcub_cherry_2414

Barisani-Asenbauer T, Inić-Kanada A, Smiljanić K, Stein E, Belaw Y, Elkheir B, Mihailović-Vesić J, Chalabi H, Schuerer N, Ghasemian E, Ćirković-Veličković T. Immunoproteomics of Relevant Chlamydial Antigens in Trachomatous Trichiasis Patients from Ethiopia and Sudan. in Investigative Ophthalmology and Visual Science. 2016;57(12).
https://hdl.handle.net/21.15107/rcub_cherry_2414 .

Barisani-Asenbauer, Talin, Inić-Kanada, Aleksandra, Smiljanić, Katarina, Stein, Elisabeth, Belaw, Yeshigeta, Elkheir, Balgesa, Mihailović-Vesić, Jelena, Chalabi, Hadeel, Schuerer, Nadine, Ghasemian, Ehsan, Ćirković-Veličković, Tanja, "Immunoproteomics of Relevant Chlamydial Antigens in Trachomatous Trichiasis Patients from Ethiopia and Sudan" in Investigative Ophthalmology and Visual Science, 57, no. 12 (2016),
https://hdl.handle.net/21.15107/rcub_cherry_2414 .

TY  - JOUR
AU  - Mihailović-Vesić, Jelena
AU  - Inić-Kanada, Aleksandra
AU  - Smiljanić, Katarina
AU  - Stein, Elisabeth
AU  - Barisani-Asenbauer, T.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/295
AB  - Chlamydia trachomatis (Ct) is a human pathogen causing trachoma and infertility. We investigated acetylation at lysine residues of chlamydial antigenic proteins: major outer membrane protein (MOMP), 60 kDa chaperonin (chlamydial Hsp60), elongation factor G (EF-G), enolase and the polymorphic membrane proteins PmpB, PmpE and PmpF. 60 kDa chaperonin, EF-G and PmpB showed the highest degree of acetylation. Our data show that important Ct antigens could be post-translationally modified by acetylation of lysine residues at multiple sites. Further studies are needed to investigate total acetylome of Ct and the impact PTMs might have on Ct biology and pathogenicity. © 2016.
T2  - EuPA Open Proteomics
T1  - Lysine acetylation of major Chlamydia trachomatis antigens
VL  - 10
SP  - 63
EP  - 69
DO  - 10.1016/j.euprot.2016.01.007
ER  - 

@article{
author = "Mihailović-Vesić, Jelena and Inić-Kanada, Aleksandra and Smiljanić, Katarina and Stein, Elisabeth and Barisani-Asenbauer, T. and Ćirković-Veličković, Tanja",
year = "2016",
abstract = "Chlamydia trachomatis (Ct) is a human pathogen causing trachoma and infertility. We investigated acetylation at lysine residues of chlamydial antigenic proteins: major outer membrane protein (MOMP), 60 kDa chaperonin (chlamydial Hsp60), elongation factor G (EF-G), enolase and the polymorphic membrane proteins PmpB, PmpE and PmpF. 60 kDa chaperonin, EF-G and PmpB showed the highest degree of acetylation. Our data show that important Ct antigens could be post-translationally modified by acetylation of lysine residues at multiple sites. Further studies are needed to investigate total acetylome of Ct and the impact PTMs might have on Ct biology and pathogenicity. © 2016.",
journal = "EuPA Open Proteomics",
title = "Lysine acetylation of major Chlamydia trachomatis antigens",
volume = "10",
pages = "63-69",
doi = "10.1016/j.euprot.2016.01.007"
}

Mihailović-Vesić, J., Inić-Kanada, A., Smiljanić, K., Stein, E., Barisani-Asenbauer, T.,& Ćirković-Veličković, T.. (2016). Lysine acetylation of major Chlamydia trachomatis antigens. in EuPA Open Proteomics, 10, 63-69.
https://doi.org/10.1016/j.euprot.2016.01.007

Mihailović-Vesić J, Inić-Kanada A, Smiljanić K, Stein E, Barisani-Asenbauer T, Ćirković-Veličković T. Lysine acetylation of major Chlamydia trachomatis antigens. in EuPA Open Proteomics. 2016;10:63-69.
doi:10.1016/j.euprot.2016.01.007 .

Mihailović-Vesić, Jelena, Inić-Kanada, Aleksandra, Smiljanić, Katarina, Stein, Elisabeth, Barisani-Asenbauer, T., Ćirković-Veličković, Tanja, "Lysine acetylation of major Chlamydia trachomatis antigens" in EuPA Open Proteomics, 10 (2016):63-69,
https://doi.org/10.1016/j.euprot.2016.01.007 . .

TY  - DATA
AU  - Mihailović-Vesić, Jelena
AU  - Stambolić, Ivan
AU  - Apostolović, Danijela
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3355
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Supplementary data for article: Vesic, J.; Stambolic, I.; Apostolovic, D.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Complexes of Green Tea Polyphenol, Epigalocatechin-3-Gallate, and 2S Albumins of Peanut. Food Chemistry 2015, 185, 309–317. https://doi.org/10.1016/j.foodchem.2015.04.001
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3355
ER  - 

@misc{
author = "Mihailović-Vesić, Jelena and Stambolić, Ivan and Apostolović, Danijela and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2015",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Supplementary data for article: Vesic, J.; Stambolic, I.; Apostolovic, D.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Complexes of Green Tea Polyphenol, Epigalocatechin-3-Gallate, and 2S Albumins of Peanut. Food Chemistry 2015, 185, 309–317. https://doi.org/10.1016/j.foodchem.2015.04.001",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3355"
}

Mihailović-Vesić, J., Stambolić, I., Apostolović, D., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2015). Supplementary data for article: Vesic, J.; Stambolic, I.; Apostolovic, D.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Complexes of Green Tea Polyphenol, Epigalocatechin-3-Gallate, and 2S Albumins of Peanut. Food Chemistry 2015, 185, 309–317. https://doi.org/10.1016/j.foodchem.2015.04.001. in Food Chemistry
Elsevier Sci Ltd, Oxford..
https://hdl.handle.net/21.15107/rcub_cherry_3355

Mihailović-Vesić J, Stambolić I, Apostolović D, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary data for article: Vesic, J.; Stambolic, I.; Apostolovic, D.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Complexes of Green Tea Polyphenol, Epigalocatechin-3-Gallate, and 2S Albumins of Peanut. Food Chemistry 2015, 185, 309–317. https://doi.org/10.1016/j.foodchem.2015.04.001. in Food Chemistry. 2015;.
https://hdl.handle.net/21.15107/rcub_cherry_3355 .

Mihailović-Vesić, Jelena, Stambolić, Ivan, Apostolović, Danijela, Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Supplementary data for article: Vesic, J.; Stambolic, I.; Apostolovic, D.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Complexes of Green Tea Polyphenol, Epigalocatechin-3-Gallate, and 2S Albumins of Peanut. Food Chemistry 2015, 185, 309–317. https://doi.org/10.1016/j.foodchem.2015.04.001" in Food Chemistry (2015),
https://hdl.handle.net/21.15107/rcub_cherry_3355 .

TY  - CONF
AU  - Minić, Simeon L.
AU  - Krstić-Ristivojević, Maja
AU  - Apostolović, Danijela
AU  - Mihailović-Vesić, Jelena
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1976
PB  - Wiley-Blackwell, Hoboken
C3  - FEBS Journal / Federation of European of Biochemical Societies
T1  - Pepsin digestion of C-phycocyanin releases chromopeptides with potent anticancer and antioxidant activities
VL  - 282
SP  - 134
EP  - 135
UR  - https://hdl.handle.net/21.15107/rcub_cherry_1976
ER  - 

@conference{
author = "Minić, Simeon L. and Krstić-Ristivojević, Maja and Apostolović, Danijela and Mihailović-Vesić, Jelena and Stanić-Vučinić, Dragana and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2015",
publisher = "Wiley-Blackwell, Hoboken",
journal = "FEBS Journal / Federation of European of Biochemical Societies",
title = "Pepsin digestion of C-phycocyanin releases chromopeptides with potent anticancer and antioxidant activities",
volume = "282",
pages = "134-135",
url = "https://hdl.handle.net/21.15107/rcub_cherry_1976"
}

Minić, S. L., Krstić-Ristivojević, M., Apostolović, D., Mihailović-Vesić, J., Stanić-Vučinić, D., Nikolić, M.,& Ćirković-Veličković, T.. (2015). Pepsin digestion of C-phycocyanin releases chromopeptides with potent anticancer and antioxidant activities. in FEBS Journal / Federation of European of Biochemical Societies
Wiley-Blackwell, Hoboken., 282, 134-135.
https://hdl.handle.net/21.15107/rcub_cherry_1976

Minić SL, Krstić-Ristivojević M, Apostolović D, Mihailović-Vesić J, Stanić-Vučinić D, Nikolić M, Ćirković-Veličković T. Pepsin digestion of C-phycocyanin releases chromopeptides with potent anticancer and antioxidant activities. in FEBS Journal / Federation of European of Biochemical Societies. 2015;282:134-135.
https://hdl.handle.net/21.15107/rcub_cherry_1976 .

Minić, Simeon L., Krstić-Ristivojević, Maja, Apostolović, Danijela, Mihailović-Vesić, Jelena, Stanić-Vučinić, Dragana, Nikolić, Milan, Ćirković-Veličković, Tanja, "Pepsin digestion of C-phycocyanin releases chromopeptides with potent anticancer and antioxidant activities" in FEBS Journal / Federation of European of Biochemical Societies, 282 (2015):134-135,
https://hdl.handle.net/21.15107/rcub_cherry_1976 .

TY  - JOUR
AU  - Mihailović-Vesić, Jelena
AU  - Stambolić, Ivan
AU  - Apostolović, Danijela
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1718
AB  - 2S albumins of peanuts are seed storage proteins, highly homologous in structure and described as major elicitors of anaphylactic reactions to peanut (allergens Ara h 2 and Ara h 6). Epigallocatechin-3-gallate (EGCG) is the most biologically potent polyphenol of green tea. Non-covalent interactions of EGCG with proteins contribute to its diverse biological activities. Here we used the methods of circular dichroism, fluorescence quenching titration, isothermal titration calorimetry and computational chemistry to elucidate interactions of EGCG and 2S albumins. Similarity in structure and overall fold of 2S albumins yielded similar putative binding sites and similar binding modes with EGCG. Binding affinity determined for Ara h 2 was in the range described for complexes of EGCG and other dietary proteins. Binding of EGCG to 2S albumins affects protein conformation, by causing an alpha-helix to beta-structures transition in both proteins. 2S albumins of peanuts may be good carriers of physiologically active green tea catechin.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Complexes of green tea polyphenol, epigalocatechin-3-gallate, and 2S albumins of peanut
VL  - 185
SP  - 309
EP  - 317
DO  - 10.1016/j.foodchem.2015.04.001
ER  - 

@article{
author = "Mihailović-Vesić, Jelena and Stambolić, Ivan and Apostolović, Danijela and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2015",
abstract = "2S albumins of peanuts are seed storage proteins, highly homologous in structure and described as major elicitors of anaphylactic reactions to peanut (allergens Ara h 2 and Ara h 6). Epigallocatechin-3-gallate (EGCG) is the most biologically potent polyphenol of green tea. Non-covalent interactions of EGCG with proteins contribute to its diverse biological activities. Here we used the methods of circular dichroism, fluorescence quenching titration, isothermal titration calorimetry and computational chemistry to elucidate interactions of EGCG and 2S albumins. Similarity in structure and overall fold of 2S albumins yielded similar putative binding sites and similar binding modes with EGCG. Binding affinity determined for Ara h 2 was in the range described for complexes of EGCG and other dietary proteins. Binding of EGCG to 2S albumins affects protein conformation, by causing an alpha-helix to beta-structures transition in both proteins. 2S albumins of peanuts may be good carriers of physiologically active green tea catechin.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Complexes of green tea polyphenol, epigalocatechin-3-gallate, and 2S albumins of peanut",
volume = "185",
pages = "309-317",
doi = "10.1016/j.foodchem.2015.04.001"
}

Mihailović-Vesić, J., Stambolić, I., Apostolović, D., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2015). Complexes of green tea polyphenol, epigalocatechin-3-gallate, and 2S albumins of peanut. in Food Chemistry
Elsevier Sci Ltd, Oxford., 185, 309-317.
https://doi.org/10.1016/j.foodchem.2015.04.001

Mihailović-Vesić J, Stambolić I, Apostolović D, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Complexes of green tea polyphenol, epigalocatechin-3-gallate, and 2S albumins of peanut. in Food Chemistry. 2015;185:309-317.
doi:10.1016/j.foodchem.2015.04.001 .

Mihailović-Vesić, Jelena, Stambolić, Ivan, Apostolović, Danijela, Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Complexes of green tea polyphenol, epigalocatechin-3-gallate, and 2S albumins of peanut" in Food Chemistry, 185 (2015):309-317,
https://doi.org/10.1016/j.foodchem.2015.04.001 . .