TY  - JOUR
AU  - Radibratović, Milica
AU  - Al-Hanish, Ayah
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3733
AB  - α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. 

EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.
PB  - Elsevier
T2  - Food Chemistry
T1  - Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study
VL  - 278
SP  - 388
EP  - 395
DO  - 10.1016/j.foodchem.2018.11.038
ER  - 

@article{
author = "Radibratović, Milica and Al-Hanish, Ayah and Minić, Simeon L. and Radomirović, Mirjana Ž. and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. 

EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study",
volume = "278",
pages = "388-395",
doi = "10.1016/j.foodchem.2018.11.038"
}

Radibratović, M., Al-Hanish, A., Minić, S. L., Radomirović, M. Ž., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2019). Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. in Food Chemistry
Elsevier., 278, 388-395.
https://doi.org/10.1016/j.foodchem.2018.11.038

Radibratović M, Al-Hanish A, Minić SL, Radomirović MŽ, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. in Food Chemistry. 2019;278:388-395.
doi:10.1016/j.foodchem.2018.11.038 .

Radibratović, Milica, Al-Hanish, Ayah, Minić, Simeon L., Radomirović, Mirjana Ž., Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study" in Food Chemistry, 278 (2019):388-395,
https://doi.org/10.1016/j.foodchem.2018.11.038 . .

TY  - JOUR
AU  - Radibratović, Milica
AU  - Al-Hanish, Ayah
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4848
AB  - α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.
PB  - Elsevier
T2  - Food Chemistry
T1  - Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study
VL  - 278
SP  - 388
EP  - 395
DO  - 10.1016/j.foodchem.2018.11.038
ER  - 

@article{
author = "Radibratović, Milica and Al-Hanish, Ayah and Minić, Simeon L. and Radomirović, Mirjana Ž. and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2019",
abstract = "α-Lactalbumin (ALA) is a Ca2+-binding protein which constitutes up to 20% of whey protein. At acidic pH, and in the apo-state at elevated temperatures, ALA is the classic 'molten globule' (MG). This study examined epigallo-catechin-3-gallate (EGCG) binding to ALA in its apo form (apoALA) and stabilizing effect on protein structure thereof. EGCG binds to apoALA in both native and MG state. The complex of EGCG and ALA is more stable to thermal denaturation. The docking analysis and molecular dynamic simulation (MDS) showed that Ca2+ removal decreased conformational stability of ALA, because of the local destabilization of Ca2+-binding region. EGCG binding to apoALA increases its stability by reverting of conformation and stability of Ca2+-binding region. Therefore, EGCG-induced thermal stability of apoALA is based on increased apoALA conformational rigidity. This study implies that during gastric digestion of tea with milk EGCG would remain bound to ALA, albeit in the Ca2+-free form.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study",
volume = "278",
pages = "388-395",
doi = "10.1016/j.foodchem.2018.11.038"
}

Radibratović, M., Al-Hanish, A., Minić, S. L., Radomirović, M. Ž., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2019). Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. in Food Chemistry
Elsevier., 278, 388-395.
https://doi.org/10.1016/j.foodchem.2018.11.038

Radibratović M, Al-Hanish A, Minić SL, Radomirović MŽ, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study. in Food Chemistry. 2019;278:388-395.
doi:10.1016/j.foodchem.2018.11.038 .

Radibratović, Milica, Al-Hanish, Ayah, Minić, Simeon L., Radomirović, Mirjana Ž., Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study" in Food Chemistry, 278 (2019):388-395,
https://doi.org/10.1016/j.foodchem.2018.11.038 . .

TY  - DATA
AU  - Radibratović, Milica
AU  - Al-Hanish, Ayah
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/4849
PB  - Elsevier
T2  - Food Chemistry
T1  - Supplementary data for the article: Radibratović, M.; Al-Hanish, A.; Minić, S. L.; Radomirović, M. Ž.; Milčić, M. K.; Stanić-Vučinić, D.; Ćirković-Veličković, T. Stabilization of Apo Alpha-Lactalbumin by Binding of Epigallocatechin-3-Gallate: Experimental and Molecular Dynamics Study. Food Chemistry 2019, 278, 388–395. https://doi.org/10.1016/j.foodchem.2018.11.038.
UR  - https://hdl.handle.net/21.15107/rcub_cherry_4849
ER  - 

@misc{
author = "Radibratović, Milica and Al-Hanish, Ayah and Minić, Simeon L. and Radomirović, Mirjana Ž. and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2019",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Supplementary data for the article: Radibratović, M.; Al-Hanish, A.; Minić, S. L.; Radomirović, M. Ž.; Milčić, M. K.; Stanić-Vučinić, D.; Ćirković-Veličković, T. Stabilization of Apo Alpha-Lactalbumin by Binding of Epigallocatechin-3-Gallate: Experimental and Molecular Dynamics Study. Food Chemistry 2019, 278, 388–395. https://doi.org/10.1016/j.foodchem.2018.11.038.",
url = "https://hdl.handle.net/21.15107/rcub_cherry_4849"
}

Radibratović, M., Al-Hanish, A., Minić, S. L., Radomirović, M. Ž., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2019). Supplementary data for the article: Radibratović, M.; Al-Hanish, A.; Minić, S. L.; Radomirović, M. Ž.; Milčić, M. K.; Stanić-Vučinić, D.; Ćirković-Veličković, T. Stabilization of Apo Alpha-Lactalbumin by Binding of Epigallocatechin-3-Gallate: Experimental and Molecular Dynamics Study. Food Chemistry 2019, 278, 388–395. https://doi.org/10.1016/j.foodchem.2018.11.038.. in Food Chemistry
Elsevier..
https://hdl.handle.net/21.15107/rcub_cherry_4849

Radibratović M, Al-Hanish A, Minić SL, Radomirović MŽ, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary data for the article: Radibratović, M.; Al-Hanish, A.; Minić, S. L.; Radomirović, M. Ž.; Milčić, M. K.; Stanić-Vučinić, D.; Ćirković-Veličković, T. Stabilization of Apo Alpha-Lactalbumin by Binding of Epigallocatechin-3-Gallate: Experimental and Molecular Dynamics Study. Food Chemistry 2019, 278, 388–395. https://doi.org/10.1016/j.foodchem.2018.11.038.. in Food Chemistry. 2019;.
https://hdl.handle.net/21.15107/rcub_cherry_4849 .

Radibratović, Milica, Al-Hanish, Ayah, Minić, Simeon L., Radomirović, Mirjana Ž., Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Supplementary data for the article: Radibratović, M.; Al-Hanish, A.; Minić, S. L.; Radomirović, M. Ž.; Milčić, M. K.; Stanić-Vučinić, D.; Ćirković-Veličković, T. Stabilization of Apo Alpha-Lactalbumin by Binding of Epigallocatechin-3-Gallate: Experimental and Molecular Dynamics Study. Food Chemistry 2019, 278, 388–395. https://doi.org/10.1016/j.foodchem.2018.11.038." in Food Chemistry (2019),
https://hdl.handle.net/21.15107/rcub_cherry_4849 .

TY  - CONF
AU  - Radibratović, Milica
AU  - Al-Hanish, Ayah
AU  - Minić, Simeon
AU  - Radomirović, Mirjana Ž.
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6040
AB  - α-Lactalbumin (ALA) is a small, acidic, Ca2+-binding protein that might constitute up to 20% of whey protein. ALA has several partially folded intermediate states. It is very attractive for studies of the properties and structure of intermediate molten globule-like states since at acidic pH and in the apo-state at elevated temperatures ALA is the classic ‘molten globule’.
The aim of our study was to examine if epi-gallo-catechin-3-gallate (EGCG) binds to ALA in its Ca-depleted (apo-ALA) and less ordered states. Moreover we examined if the polyphenol binding can stabilize protein structure. The experimental investigation of EGCG binding and protein’s stability were supported by molecular dynamics data.
Green tea catechin binds to apo-ALA in neutral and acidic conditions. Binding affinity determined by intrinsic fluorescence quenching is of a similar magnitude as to the holo form of the protein. The complex of EGCG and ALA at neutral conditions is more stable to thermal denaturation then protein alone. The stabilizing effect is more pronounced for apo-ALA than for the holo-ALA.
The docking analysis and molecular dynamic simulation (MDS) showed that EGCG binds to apoALA at the same site as to holoALA, in the hydrophobic pocket at the entrance of cleft between α and β subdomains, remaining bound during MDS. Ca2+ removal results in decreased conformational stability of ALA, where local destabilization of Ca2+-binding region propagates to cleft, with its slight opening. EGCG binding to apo-ALA increases stability of ALA by reverting of conformation and stability of disturbed Ca2+-binding region, which is transmitted to cleft, resulting in rejoining of α and β subdomains and slight cleft closing by the same mechanism. EGCG binding could retard transition of apo-ALA to less ordered states under conditions favoring its formation.
Therefore, non-covalent binding of EGCG can stabilize structural fold of calcium-depleted ALA.
PB  - Univerzitet u Beogradu
C3  - UNIFOOD Conference, Belgrade, Serbia, 5th–6th October, 2018. In: UNIFOOD Conference - Programme and Book of Abstracts
T1  - Stabilization of apo-alpha-lactalbumin by binding of epigallocatechin-3-gallate: experimental and molecular dynamics study
SP  - 268
EP  - 268
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6040
ER  - 

@conference{
author = "Radibratović, Milica and Al-Hanish, Ayah and Minić, Simeon and Radomirović, Mirjana Ž. and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "α-Lactalbumin (ALA) is a small, acidic, Ca2+-binding protein that might constitute up to 20% of whey protein. ALA has several partially folded intermediate states. It is very attractive for studies of the properties and structure of intermediate molten globule-like states since at acidic pH and in the apo-state at elevated temperatures ALA is the classic ‘molten globule’.
The aim of our study was to examine if epi-gallo-catechin-3-gallate (EGCG) binds to ALA in its Ca-depleted (apo-ALA) and less ordered states. Moreover we examined if the polyphenol binding can stabilize protein structure. The experimental investigation of EGCG binding and protein’s stability were supported by molecular dynamics data.
Green tea catechin binds to apo-ALA in neutral and acidic conditions. Binding affinity determined by intrinsic fluorescence quenching is of a similar magnitude as to the holo form of the protein. The complex of EGCG and ALA at neutral conditions is more stable to thermal denaturation then protein alone. The stabilizing effect is more pronounced for apo-ALA than for the holo-ALA.
The docking analysis and molecular dynamic simulation (MDS) showed that EGCG binds to apoALA at the same site as to holoALA, in the hydrophobic pocket at the entrance of cleft between α and β subdomains, remaining bound during MDS. Ca2+ removal results in decreased conformational stability of ALA, where local destabilization of Ca2+-binding region propagates to cleft, with its slight opening. EGCG binding to apo-ALA increases stability of ALA by reverting of conformation and stability of disturbed Ca2+-binding region, which is transmitted to cleft, resulting in rejoining of α and β subdomains and slight cleft closing by the same mechanism. EGCG binding could retard transition of apo-ALA to less ordered states under conditions favoring its formation.
Therefore, non-covalent binding of EGCG can stabilize structural fold of calcium-depleted ALA.",
publisher = "Univerzitet u Beogradu",
journal = "UNIFOOD Conference, Belgrade, Serbia, 5th–6th October, 2018. In: UNIFOOD Conference - Programme and Book of Abstracts",
title = "Stabilization of apo-alpha-lactalbumin by binding of epigallocatechin-3-gallate: experimental and molecular dynamics study",
pages = "268-268",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6040"
}

Radibratović, M., Al-Hanish, A., Minić, S., Radomirović, M. Ž., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2018). Stabilization of apo-alpha-lactalbumin by binding of epigallocatechin-3-gallate: experimental and molecular dynamics study. in UNIFOOD Conference, Belgrade, Serbia, 5th–6th October, 2018. In: UNIFOOD Conference - Programme and Book of Abstracts
Univerzitet u Beogradu., 268-268.
https://hdl.handle.net/21.15107/rcub_cherry_6040

Radibratović M, Al-Hanish A, Minić S, Radomirović MŽ, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Stabilization of apo-alpha-lactalbumin by binding of epigallocatechin-3-gallate: experimental and molecular dynamics study. in UNIFOOD Conference, Belgrade, Serbia, 5th–6th October, 2018. In: UNIFOOD Conference - Programme and Book of Abstracts. 2018;:268-268.
https://hdl.handle.net/21.15107/rcub_cherry_6040 .

Radibratović, Milica, Al-Hanish, Ayah, Minić, Simeon, Radomirović, Mirjana Ž., Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Stabilization of apo-alpha-lactalbumin by binding of epigallocatechin-3-gallate: experimental and molecular dynamics study" in UNIFOOD Conference, Belgrade, Serbia, 5th–6th October, 2018. In: UNIFOOD Conference - Programme and Book of Abstracts (2018):268-268,
https://hdl.handle.net/21.15107/rcub_cherry_6040 .

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  - 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  - 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  - Peruško, Marija
AU  - Al-Hanish, Ayah
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2015
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/5262
AB  - High intensity ultrasound (HIUS) can promote Maillard reaction (MR). Macromolecular crowding conditions accelerate reactions and stabilise protein structure. The aim of this study was to investigate if combined application of ultrasound and macromolecular crowding can improve efficiency of MR. The presence of crowding agent (polyethylene glycol) significantly increased ultrasound-induced whey protein (WP) glycation by arabinose. An increase in glycation efficiency results only in slight change of WP structure. Macromolecular crowding intensifies oxidative modifications of WP, as well as formation of amyloid-like structures by enhancement of MR. Solubility at different pH, thermal stability and antioxidative capacity of glycated WP were increased, especially in the presence of crowding agent, compared to sonicated nonglycated proteins. The application of HIUS under crowding conditions can be a new approach for enhancement of reactions in general, enabling short processing time and mild conditions, while preserving protein structure and minimising protein aggregation. (C) 2015 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction
VL  - 177
SP  - 248
EP  - 257
DO  - 10.1016/j.foodchem.2015.01.042
ER  - 

@article{
author = "Peruško, Marija and Al-Hanish, Ayah and Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2015",
abstract = "High intensity ultrasound (HIUS) can promote Maillard reaction (MR). Macromolecular crowding conditions accelerate reactions and stabilise protein structure. The aim of this study was to investigate if combined application of ultrasound and macromolecular crowding can improve efficiency of MR. The presence of crowding agent (polyethylene glycol) significantly increased ultrasound-induced whey protein (WP) glycation by arabinose. An increase in glycation efficiency results only in slight change of WP structure. Macromolecular crowding intensifies oxidative modifications of WP, as well as formation of amyloid-like structures by enhancement of MR. Solubility at different pH, thermal stability and antioxidative capacity of glycated WP were increased, especially in the presence of crowding agent, compared to sonicated nonglycated proteins. The application of HIUS under crowding conditions can be a new approach for enhancement of reactions in general, enabling short processing time and mild conditions, while preserving protein structure and minimising protein aggregation. (C) 2015 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction",
volume = "177",
pages = "248-257",
doi = "10.1016/j.foodchem.2015.01.042"
}

Peruško, M., Al-Hanish, A., Ćirković-Veličković, T.,& Stanić-Vučinić, D.. (2015). Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction. in Food Chemistry
Elsevier Sci Ltd, Oxford., 177, 248-257.
https://doi.org/10.1016/j.foodchem.2015.01.042

Peruško M, Al-Hanish A, Ćirković-Veličković T, Stanić-Vučinić D. Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction. in Food Chemistry. 2015;177:248-257.
doi:10.1016/j.foodchem.2015.01.042 .

Peruško, Marija, Al-Hanish, Ayah, Ćirković-Veličković, Tanja, Stanić-Vučinić, Dragana, "Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction" in Food Chemistry, 177 (2015):248-257,
https://doi.org/10.1016/j.foodchem.2015.01.042 . .

TY  - JOUR
AU  - Peruško, Marija
AU  - Al-Hanish, Ayah
AU  - Ćirković-Veličković, Tanja
AU  - Stanić-Vučinić, Dragana
PY  - 2015
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1666
AB  - High intensity ultrasound (HIUS) can promote Maillard reaction (MR). Macromolecular crowding conditions accelerate reactions and stabilise protein structure. The aim of this study was to investigate if combined application of ultrasound and macromolecular crowding can improve efficiency of MR. The presence of crowding agent (polyethylene glycol) significantly increased ultrasound-induced whey protein (WP) glycation by arabinose. An increase in glycation efficiency results only in slight change of WP structure. Macromolecular crowding intensifies oxidative modifications of WP, as well as formation of amyloid-like structures by enhancement of MR. Solubility at different pH, thermal stability and antioxidative capacity of glycated WP were increased, especially in the presence of crowding agent, compared to sonicated nonglycated proteins. The application of HIUS under crowding conditions can be a new approach for enhancement of reactions in general, enabling short processing time and mild conditions, while preserving protein structure and minimising protein aggregation. (C) 2015 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction
VL  - 177
SP  - 248
EP  - 257
DO  - 10.1016/j.foodchem.2015.01.042
ER  - 

@article{
author = "Peruško, Marija and Al-Hanish, Ayah and Ćirković-Veličković, Tanja and Stanić-Vučinić, Dragana",
year = "2015",
abstract = "High intensity ultrasound (HIUS) can promote Maillard reaction (MR). Macromolecular crowding conditions accelerate reactions and stabilise protein structure. The aim of this study was to investigate if combined application of ultrasound and macromolecular crowding can improve efficiency of MR. The presence of crowding agent (polyethylene glycol) significantly increased ultrasound-induced whey protein (WP) glycation by arabinose. An increase in glycation efficiency results only in slight change of WP structure. Macromolecular crowding intensifies oxidative modifications of WP, as well as formation of amyloid-like structures by enhancement of MR. Solubility at different pH, thermal stability and antioxidative capacity of glycated WP were increased, especially in the presence of crowding agent, compared to sonicated nonglycated proteins. The application of HIUS under crowding conditions can be a new approach for enhancement of reactions in general, enabling short processing time and mild conditions, while preserving protein structure and minimising protein aggregation. (C) 2015 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction",
volume = "177",
pages = "248-257",
doi = "10.1016/j.foodchem.2015.01.042"
}

Peruško, M., Al-Hanish, A., Ćirković-Veličković, T.,& Stanić-Vučinić, D.. (2015). Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction. in Food Chemistry
Elsevier Sci Ltd, Oxford., 177, 248-257.
https://doi.org/10.1016/j.foodchem.2015.01.042

Peruško M, Al-Hanish A, Ćirković-Veličković T, Stanić-Vučinić D. Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction. in Food Chemistry. 2015;177:248-257.
doi:10.1016/j.foodchem.2015.01.042 .

Peruško, Marija, Al-Hanish, Ayah, Ćirković-Veličković, Tanja, Stanić-Vučinić, Dragana, "Macromolecular crowding conditions enhance glycation and oxidation of whey proteins in ultrasound-induced Maillard reaction" in Food Chemistry, 177 (2015):248-257,
https://doi.org/10.1016/j.foodchem.2015.01.042 . .