Minić, Simeon L.

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orcid::0000-0002-7053-1216
  • Minić, Simeon L. (29)

Author's Bibliography

Stabilization of apo alpha-lactalbumin by binding of epigallocatechin-3-gallate: Experimental and molecular dynamics study

Radibratović, Milica; Al-Hanish, Ayah; Minić, Simeon L.; Radomirović, Mirjana Ž.; Milčić, Miloš K.; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Elsevier, 2019)

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/123456789/3733
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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3733",
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.
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. Food Chemistry. 2019;278:388-395
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" Food Chemistry, 278 (2019):388-395,
https://doi.org/10.1016/j.foodchem.2018.11.038 .
3
3
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Characterisation and the effects of bilirubin binding to human fibrinogen

Gligorijević, Nikola; Minić, Simeon L.; Robajac, Dragana B.; Nikolić, Milan; Ćirković-Veličković, Tanja; Nedić, Olgica

(2019)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Robajac, Dragana B.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
AU  - Nedić, Olgica
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2824
AB  - Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventing its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction.
T2  - International Journal of Biological Macromolecules
T1  - Characterisation and the effects of bilirubin binding to human fibrinogen
VL  - 128
SP  - 74
EP  - 79
DO  - 10.1016/j.ijbiomac.2019.01.124
ER  - 
@article{
author = "Gligorijević, Nikola and Minić, Simeon L. and Robajac, Dragana B. and Nikolić, Milan and Ćirković-Veličković, Tanja and Nedić, Olgica",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2824",
abstract = "Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventing its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction.",
journal = "International Journal of Biological Macromolecules",
title = "Characterisation and the effects of bilirubin binding to human fibrinogen",
volume = "128",
pages = "74-79",
doi = "10.1016/j.ijbiomac.2019.01.124"
}
Gligorijević, N., Minić, S. L., Robajac, D. B., Nikolić, M., Ćirković-Veličković, T.,& Nedić, O. (2019). Characterisation and the effects of bilirubin binding to human fibrinogen.
International Journal of Biological Macromolecules, 128, 74-79.
https://doi.org/10.1016/j.ijbiomac.2019.01.124
Gligorijević N, Minić SL, Robajac DB, Nikolić M, Ćirković-Veličković T, Nedić O. Characterisation and the effects of bilirubin binding to human fibrinogen. International Journal of Biological Macromolecules. 2019;128:74-79
Gligorijević Nikola, Minić Simeon L., Robajac Dragana B., Nikolić Milan, Ćirković-Veličković Tanja, Nedić Olgica, "Characterisation and the effects of bilirubin binding to human fibrinogen" International Journal of Biological Macromolecules, 128 (2019):74-79,
https://doi.org/10.1016/j.ijbiomac.2019.01.124 .
6
5
6

Characterisation and the effects of bilirubin binding to human fibrinogen

Gligorijević, Nikola; Minić, Simeon L.; Robajac, Dragana B.; Nikolić, Milan; Ćirković-Veličković, Tanja; Nedić, Olgica

(2019)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Robajac, Dragana B.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
AU  - Nedić, Olgica
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2825
AB  - Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventing its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction.
T2  - International Journal of Biological Macromolecules
T1  - Characterisation and the effects of bilirubin binding to human fibrinogen
VL  - 128
SP  - 74
EP  - 79
DO  - 10.1016/j.ijbiomac.2019.01.124
ER  - 
@article{
author = "Gligorijević, Nikola and Minić, Simeon L. and Robajac, Dragana B. and Nikolić, Milan and Ćirković-Veličković, Tanja and Nedić, Olgica",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2825",
abstract = "Fibrinogen, a protein involved in blood coagulation, is very susceptible to oxidation. Oxidation alters its function and usually makes it more thrombogenic. Bilirubin, an end-product of the haem degradation in vertebrates, is known for its antioxidant properties. The present paper describes interaction between fibrinogen and bilirubin, and the influence of bilirubin on the formation of fibrin and protection against oxidation. The binding constant of 4.5 × 104 M−1 was determined for the fibrinogen/bilirubin complex at 37 °C. There is no change in secondary and tertiary structure of fibrinogen or its thermal stability upon bilirubin binding. The binding site of fibrinogen is not stereospecific for bilirubin and is able to accommodate both bilirubin conformers. A change in absorption maximum of bilirubin occurs upon its interaction with fibrinogen, suggesting an alteration in the conformation of bilirubin to the more cyclic one. Bilirubin exerts antioxidant effect on fibrinogen, preventing its carbonylation and aggregation. The presence of bilirubin induces the formation of fibrin with thicker fibres, as assessed by the coagulation assay. Fibrinogen and bilirubin interact at physiological concentrations, bilirubin may act as an antioxidant for fibrinogen and may modulate an important event in haemostasis, which altogether suggests possible physiological relevance of this interaction.",
journal = "International Journal of Biological Macromolecules",
title = "Characterisation and the effects of bilirubin binding to human fibrinogen",
volume = "128",
pages = "74-79",
doi = "10.1016/j.ijbiomac.2019.01.124"
}
Gligorijević, N., Minić, S. L., Robajac, D. B., Nikolić, M., Ćirković-Veličković, T.,& Nedić, O. (2019). Characterisation and the effects of bilirubin binding to human fibrinogen.
International Journal of Biological Macromolecules, 128, 74-79.
https://doi.org/10.1016/j.ijbiomac.2019.01.124
Gligorijević N, Minić SL, Robajac DB, Nikolić M, Ćirković-Veličković T, Nedić O. Characterisation and the effects of bilirubin binding to human fibrinogen. International Journal of Biological Macromolecules. 2019;128:74-79
Gligorijević Nikola, Minić Simeon L., Robajac Dragana B., Nikolić Milan, Ćirković-Veličković Tanja, Nedić Olgica, "Characterisation and the effects of bilirubin binding to human fibrinogen" International Journal of Biological Macromolecules, 128 (2019):74-79,
https://doi.org/10.1016/j.ijbiomac.2019.01.124 .
6
5
6

Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124

Gligorijević, Nikola; Minić, Simeon L.; Robajac, Dragana B.; Nikolić, Milan; Ćirković-Veličković, Tanja; Nedić, Olgica

(2019)

TY  - BOOK
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Robajac, Dragana B.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
AU  - Nedić, Olgica
PY  - 2019
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2937
T2  - International Journal of Biological Macromolecules
T1  - Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124
ER  - 
@book{
author = "Gligorijević, Nikola and Minić, Simeon L. and Robajac, Dragana B. and Nikolić, Milan and Ćirković-Veličković, Tanja and Nedić, Olgica",
year = "2019",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2937",
journal = "International Journal of Biological Macromolecules",
title = "Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124"
}
Gligorijević, N., Minić, S. L., Robajac, D. B., Nikolić, M., Ćirković-Veličković, T.,& Nedić, O. (2019). Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124.
International Journal of Biological Macromolecules.
Gligorijević N, Minić SL, Robajac DB, Nikolić M, Ćirković-Veličković T, Nedić O. Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124. International Journal of Biological Macromolecules. 2019;
Gligorijević Nikola, Minić Simeon L., Robajac Dragana B., Nikolić Milan, Ćirković-Veličković Tanja, Nedić Olgica, "Supplementary data for the article: Gligorijević, N.; Minić, S. L.; Robajac, D. B.; Nikolić, M.; Ćirković-Veličković, T.; Nedić, O. Characterisation and the Effects of Bilirubin Binding to Human Fibrinogen. International Journal of Biological Macromolecules 2019, 128, 74–79. https://doi.org/10.1016/j.ijbiomac.2019.01.124" International Journal of Biological Macromolecules (2019)

Redox properties of transitional milk from mothers of preterm infants

Minić, Simeon L.; Ješić, Miloš; Đurović, Dijana; Miletić, Srđan B.; Lugonja, Nikoleta; Marinković, Vesna; Nikolić-Kokić, Aleksandra; Spasić, Snežana; Vrvić, Miroslav M.

(Wiley, Hoboken, 2018)

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Ješić, Miloš
AU  - Đurović, Dijana
AU  - Miletić, Srđan B.
AU  - Lugonja, Nikoleta
AU  - Marinković, Vesna
AU  - Nikolić-Kokić, Aleksandra
AU  - Spasić, Snežana
AU  - Vrvić, Miroslav M.
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2084
AB  - AimThere is a discrepancy between the amount of transitional milk produced by mothers of preterm infants and the low capacity of premature infants to consume it. This milk can be used in milk banks, but previous studies found that there are large variations in the level of host-defence proteins in individual samples of milk from mothers of premature infants, which implies that large individual variations in antioxidative defence composition are also possible. MethodsMilk samples were collected from 20 healthy mothers of preterm infants. We determined the values for non-enzymatic antioxidative capacity parameters (oxygen radical absorbance capacity (ORAC)), static oxidation-reduction potential (ORP), activities of antioxidant defence enzymes and the amount of vitamin C in whole milk, skim and whey fractions of transitional milk. ResultsThe main low-molecular-weight antioxidant in transitional milk is vitamin C and most of it is contained in whey. ORAC is higher in whole transitional milk than in skim milk and whey, and ORP is lower in whole transitional milk than that in skim milk and whey. Antioxidative enzyme activities are similar in all individual samples of transitional milk from mothers of preterm infants. ConclusionsOur results indicate that transitional milk of mothers of preterm infants shows slow individual variations in antioxidative defence composition; therefore, it can be used in human milk banks.
PB  - Wiley, Hoboken
T2  - Journal of Paediatrics and Child Health
T1  - Redox properties of transitional milk from mothers of preterm infants
VL  - 54
IS  - 2
SP  - 160
EP  - 164
DO  - 10.1111/jpc.13676
ER  - 
@article{
author = "Minić, Simeon L. and Ješić, Miloš and Đurović, Dijana and Miletić, Srđan B. and Lugonja, Nikoleta and Marinković, Vesna and Nikolić-Kokić, Aleksandra and Spasić, Snežana and Vrvić, Miroslav M.",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2084",
abstract = "AimThere is a discrepancy between the amount of transitional milk produced by mothers of preterm infants and the low capacity of premature infants to consume it. This milk can be used in milk banks, but previous studies found that there are large variations in the level of host-defence proteins in individual samples of milk from mothers of premature infants, which implies that large individual variations in antioxidative defence composition are also possible. MethodsMilk samples were collected from 20 healthy mothers of preterm infants. We determined the values for non-enzymatic antioxidative capacity parameters (oxygen radical absorbance capacity (ORAC)), static oxidation-reduction potential (ORP), activities of antioxidant defence enzymes and the amount of vitamin C in whole milk, skim and whey fractions of transitional milk. ResultsThe main low-molecular-weight antioxidant in transitional milk is vitamin C and most of it is contained in whey. ORAC is higher in whole transitional milk than in skim milk and whey, and ORP is lower in whole transitional milk than that in skim milk and whey. Antioxidative enzyme activities are similar in all individual samples of transitional milk from mothers of preterm infants. ConclusionsOur results indicate that transitional milk of mothers of preterm infants shows slow individual variations in antioxidative defence composition; therefore, it can be used in human milk banks.",
publisher = "Wiley, Hoboken",
journal = "Journal of Paediatrics and Child Health",
title = "Redox properties of transitional milk from mothers of preterm infants",
volume = "54",
number = "2",
pages = "160-164",
doi = "10.1111/jpc.13676"
}
Minić, S. L., Ješić, M., Đurović, D., Miletić, S. B., Lugonja, N., Marinković, V., Nikolić-Kokić, A., Spasić, S.,& Vrvić, M. M. (2018). Redox properties of transitional milk from mothers of preterm infants.
Journal of Paediatrics and Child Health
Wiley, Hoboken., 54(2), 160-164.
https://doi.org/10.1111/jpc.13676
Minić SL, Ješić M, Đurović D, Miletić SB, Lugonja N, Marinković V, Nikolić-Kokić A, Spasić S, Vrvić MM. Redox properties of transitional milk from mothers of preterm infants. Journal of Paediatrics and Child Health. 2018;54(2):160-164
Minić Simeon L., Ješić Miloš, Đurović Dijana, Miletić Srđan B., Lugonja Nikoleta, Marinković Vesna, Nikolić-Kokić Aleksandra, Spasić Snežana, Vrvić Miroslav M., "Redox properties of transitional milk from mothers of preterm infants" Journal of Paediatrics and Child Health, 54, no. 2 (2018):160-164,
https://doi.org/10.1111/jpc.13676 .
4
2
1
3

Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.; Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099. https://doi.org/10.1016/j.foodchem.2017.07.066

Minić, Simeon L.; Stanić-Vučinić, Dragana; Radomirović, Mirjana Ž.; Radibratović, Milica; Milčić, Miloš K.; Nikolić, Milan; Ćirković-Veličković, Tanja

(Elsevier, 2018)

TY  - BOOK
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana Ž.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3139
PB  - Elsevier
T2  - Food Chemistry
T1  - Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066
ER  - 
@book{
author = "Minić, Simeon L. and Stanić-Vučinić, Dragana and Radomirović, Mirjana Ž. and Radibratović, Milica and Milčić, Miloš K. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3139",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066"
}
Minić, S. L., Stanić-Vučinić, D., Radomirović, M. Ž., Radibratović, M., Milčić, M. K., Nikolić, M.,& Ćirković-Veličković, T. (2018). Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066.
Food Chemistry
Elsevier..
Minić SL, Stanić-Vučinić D, Radomirović MŽ, Radibratović M, Milčić MK, Nikolić M, Ćirković-Veličković T. Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066. Food Chemistry. 2018;
Minić Simeon L., Stanić-Vučinić Dragana, Radomirović Mirjana Ž., Radibratović Milica, Milčić Miloš K., Nikolić Milan, Ćirković-Veličković Tanja, "Supplementary material for the article: Minic, S.; Stanic-Vucinic, D.; Radomirovic, M.; Radibratovic, M.; Milcic, M.; Nikolic, M.;  Cirkovic Velickovic, T. Characterization and Effects of Binding of Food-Derived Bioactive  Phycocyanobilin to Bovine Serum Albumin. Food Chemistry 2018, 239, 1090–1099.  https://doi.org/10.1016/j.foodchem.2017.07.066" Food Chemistry (2018)

Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions

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

(Elsevier Sci Ltd, Oxford, 2018)

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  - http://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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3186",
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.
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. Food Chemistry. 2018;269:43-52
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" Food Chemistry, 269 (2018):43-52,
https://doi.org/10.1016/j.foodchem.2018.06.138 .
1
3
2
2

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

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

(Elsevier Sci Ltd, Oxford, 2018)

TY  - BOOK
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  - http://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
ER  - 
@book{
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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3187",
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"
}
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.
Food Chemistry
Elsevier Sci Ltd, Oxford..
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. Food Chemistry. 2018;
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" Food Chemistry (2018)

Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects

Radomirović, Mirjana Ž.; Minić, Simeon L.; Savković, Nina; Vasović, T.; Nikolić, Milan; Stanić-Vučinić, Dragana; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2018)

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Minić, Simeon L.
AU  - Savković, Nina
AU  - Vasović, T.
AU  - Nikolić, Milan
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2175
PB  - Wiley, Hoboken
C3  - FEBS OPEN BIO
T1  - Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects
VL  - 8
SP  - 97
EP  - 97
ER  - 
@conference{
author = "Radomirović, Mirjana Ž. and Minić, Simeon L. and Savković, Nina and Vasović, T. and Nikolić, Milan and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2175",
publisher = "Wiley, Hoboken",
journal = "FEBS OPEN BIO",
title = "Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects",
volume = "8",
pages = "97-97"
}
Radomirović, M. Ž., Minić, S. L., Savković, N., Vasović, T., Nikolić, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T. (2018). Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects.
FEBS OPEN BIO
Wiley, Hoboken., 8, 97-97.
Radomirović MŽ, Minić SL, Savković N, Vasović T, Nikolić M, Stanić-Vučinić D, Ćirković-Veličković T. Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects. FEBS OPEN BIO. 2018;8:97-97
Radomirović Mirjana Ž., Minić Simeon L., Savković Nina, Vasović T., Nikolić Milan, Stanić-Vučinić Dragana, Ćirković-Veličković Tanja, "Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects" FEBS OPEN BIO, 8 (2018):97-97

Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions

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

(Elsevier Sci Ltd, Oxford, 2018)

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  - http://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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2197",
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.
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. Food Chemistry. 2018;269:43-52
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" Food Chemistry, 269 (2018):43-52,
https://doi.org/10.1016/j.foodchem.2018.06.138 .
1
3
2
2

Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin

Minić, Simeon L.; Stanić-Vučinić, Dragana; Radomirović, Mirjana Ž.; Radibratović, Milica; Milčić, Miloš K.; Nikolić, Milan; Ćirković-Veličković, Tanja

(Elsevier, 2018)

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana Ž.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2515
AB  - Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (K-a = 2 x 10(6) M-1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin. (C) 2017 Elsevier Ltd. All rights reserved.
PB  - Elsevier
T2  - Food Chemistry
T1  - Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin
VL  - 239
SP  - 1090
EP  - 1099
DO  - 10.1016/j.foodchem.2017.07.066
ER  - 
@article{
author = "Minić, Simeon L. and Stanić-Vučinić, Dragana and Radomirović, Mirjana Ž. and Radibratović, Milica and Milčić, Miloš K. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2515",
abstract = "Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (K-a = 2 x 10(6) M-1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin. (C) 2017 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin",
volume = "239",
pages = "1090-1099",
doi = "10.1016/j.foodchem.2017.07.066"
}
Minić, S. L., Stanić-Vučinić, D., Radomirović, M. Ž., Radibratović, M., Milčić, M. K., Nikolić, M.,& Ćirković-Veličković, T. (2018). Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin.
Food Chemistry
Elsevier., 239, 1090-1099.
https://doi.org/10.1016/j.foodchem.2017.07.066
Minić SL, Stanić-Vučinić D, Radomirović MŽ, Radibratović M, Milčić MK, Nikolić M, Ćirković-Veličković T. Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. Food Chemistry. 2018;239:1090-1099
Minić Simeon L., Stanić-Vučinić Dragana, Radomirović Mirjana Ž., Radibratović Milica, Milčić Miloš K., Nikolić Milan, Ćirković-Veličković Tanja, "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin" Food Chemistry, 239 (2018):1090-1099,
https://doi.org/10.1016/j.foodchem.2017.07.066 .
18
17
19

Structural changes of fibrinogen as a consequence of cirrhosis

Gligorijević, Nikola; Minić, Simeon L.; Krizakova, Martina; Katrlik, Jaroslav; Nedić, Olgica

(Pergamon-Elsevier Science Ltd, Oxford, 2018)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Krizakova, Martina
AU  - Katrlik, Jaroslav
AU  - Nedić, Olgica
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2142
AB  - Cirrhosis is a disease which may develop as a consequence of various conditions. In advanced liver disease, blood coagulation can be seriously affected. Portal hypertension, vascular abnormalities and/or a dysbalance in coagulation factors may result in bleeding disorders or in the development of thrombosis. Fibrinogen is the main protein involved in clot formation and wound healing. The aim of this work was to analyse the glycosylation pattern of the isolated fibrinogen molecules by lectin-based protein microarray, together with the carbonylation pattern of the individual fibrinogen chains, possible changes in the molecular secondary and tertiary structure and reactivity with the insulin-like growth factor-binding protein 1 (IGFBP-1) in patients with cirrhosis. The results pointed to an increase in several carbohydrate moieties: tri/tetra-antennary structures, Gal beta-1,4 GlcNAc, terminal alpha-2,3 Sia and alpha-1,3 Man, and a decrease in core alpha-1,6 Fuc and bi-antennary galactosylated N-glycans with bisecting GlcNAc. Fibrinogen A alpha chain was the most susceptible to carbonylation, followed by the B beta chain. Cirrhosis induced additional protein carbonylation, mostly on the alpha chain. Spectrofluorimetry and CD spectrometry detected reduction in the alpha-helix content, protein unfolding and/or appearance of modified amino acid residues in cirrhosis. The amount of complexes which fibrinogen forms with IGFBP-1, another factor involved in wound healing was significantly greater in patients with cirrhosis than in healthy individuals. A more detailed knowledge of individual molecules in coagulation process may contribute to deeper understanding of coagulopathies and the results of this study offer additional information on the possible mechanisms involved in impaired coagulation due to cirrhosis.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Thrombosis Research
T1  - Structural changes of fibrinogen as a consequence of cirrhosis
VL  - 166
SP  - 43
EP  - 49
DO  - 10.1016/j.thromres.2018.04.005
ER  - 
@article{
author = "Gligorijević, Nikola and Minić, Simeon L. and Krizakova, Martina and Katrlik, Jaroslav and Nedić, Olgica",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2142",
abstract = "Cirrhosis is a disease which may develop as a consequence of various conditions. In advanced liver disease, blood coagulation can be seriously affected. Portal hypertension, vascular abnormalities and/or a dysbalance in coagulation factors may result in bleeding disorders or in the development of thrombosis. Fibrinogen is the main protein involved in clot formation and wound healing. The aim of this work was to analyse the glycosylation pattern of the isolated fibrinogen molecules by lectin-based protein microarray, together with the carbonylation pattern of the individual fibrinogen chains, possible changes in the molecular secondary and tertiary structure and reactivity with the insulin-like growth factor-binding protein 1 (IGFBP-1) in patients with cirrhosis. The results pointed to an increase in several carbohydrate moieties: tri/tetra-antennary structures, Gal beta-1,4 GlcNAc, terminal alpha-2,3 Sia and alpha-1,3 Man, and a decrease in core alpha-1,6 Fuc and bi-antennary galactosylated N-glycans with bisecting GlcNAc. Fibrinogen A alpha chain was the most susceptible to carbonylation, followed by the B beta chain. Cirrhosis induced additional protein carbonylation, mostly on the alpha chain. Spectrofluorimetry and CD spectrometry detected reduction in the alpha-helix content, protein unfolding and/or appearance of modified amino acid residues in cirrhosis. The amount of complexes which fibrinogen forms with IGFBP-1, another factor involved in wound healing was significantly greater in patients with cirrhosis than in healthy individuals. A more detailed knowledge of individual molecules in coagulation process may contribute to deeper understanding of coagulopathies and the results of this study offer additional information on the possible mechanisms involved in impaired coagulation due to cirrhosis.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Thrombosis Research",
title = "Structural changes of fibrinogen as a consequence of cirrhosis",
volume = "166",
pages = "43-49",
doi = "10.1016/j.thromres.2018.04.005"
}
Gligorijević, N., Minić, S. L., Krizakova, M., Katrlik, J.,& Nedić, O. (2018). Structural changes of fibrinogen as a consequence of cirrhosis.
Thrombosis Research
Pergamon-Elsevier Science Ltd, Oxford., 166, 43-49.
https://doi.org/10.1016/j.thromres.2018.04.005
Gligorijević N, Minić SL, Krizakova M, Katrlik J, Nedić O. Structural changes of fibrinogen as a consequence of cirrhosis. Thrombosis Research. 2018;166:43-49
Gligorijević Nikola, Minić Simeon L., Krizakova Martina, Katrlik Jaroslav, Nedić Olgica, "Structural changes of fibrinogen as a consequence of cirrhosis" Thrombosis Research, 166 (2018):43-49,
https://doi.org/10.1016/j.thromres.2018.04.005 .
4
4
4

Structural changes of fibrinogen as a consequence of cirrhosis

Gligorijević, Nikola; Minić, Simeon L.; Krizakova, Martina; Katrlik, Jaroslav; Nedić, Olgica

(Pergamon-Elsevier Science Ltd, Oxford, 2018)

TY  - JOUR
AU  - Gligorijević, Nikola
AU  - Minić, Simeon L.
AU  - Krizakova, Martina
AU  - Katrlik, Jaroslav
AU  - Nedić, Olgica
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3265
AB  - Cirrhosis is a disease which may develop as a consequence of various conditions. In advanced liver disease, blood coagulation can be seriously affected. Portal hypertension, vascular abnormalities and/or a dysbalance in coagulation factors may result in bleeding disorders or in the development of thrombosis. Fibrinogen is the main protein involved in clot formation and wound healing. The aim of this work was to analyse the glycosylation pattern of the isolated fibrinogen molecules by lectin-based protein microarray, together with the carbonylation pattern of the individual fibrinogen chains, possible changes in the molecular secondary and tertiary structure and reactivity with the insulin-like growth factor-binding protein 1 (IGFBP-1) in patients with cirrhosis. The results pointed to an increase in several carbohydrate moieties: tri/tetra-antennary structures, Gal beta-1,4 GlcNAc, terminal alpha-2,3 Sia and alpha-1,3 Man, and a decrease in core alpha-1,6 Fuc and bi-antennary galactosylated N-glycans with bisecting GlcNAc. Fibrinogen A alpha chain was the most susceptible to carbonylation, followed by the B beta chain. Cirrhosis induced additional protein carbonylation, mostly on the alpha chain. Spectrofluorimetry and CD spectrometry detected reduction in the alpha-helix content, protein unfolding and/or appearance of modified amino acid residues in cirrhosis. The amount of complexes which fibrinogen forms with IGFBP-1, another factor involved in wound healing was significantly greater in patients with cirrhosis than in healthy individuals. A more detailed knowledge of individual molecules in coagulation process may contribute to deeper understanding of coagulopathies and the results of this study offer additional information on the possible mechanisms involved in impaired coagulation due to cirrhosis.
PB  - Pergamon-Elsevier Science Ltd, Oxford
T2  - Thrombosis Research
T1  - Structural changes of fibrinogen as a consequence of cirrhosis
VL  - 166
SP  - 43
EP  - 49
DO  - 10.1016/j.thromres.2018.04.005
ER  - 
@article{
author = "Gligorijević, Nikola and Minić, Simeon L. and Krizakova, Martina and Katrlik, Jaroslav and Nedić, Olgica",
year = "2018",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3265",
abstract = "Cirrhosis is a disease which may develop as a consequence of various conditions. In advanced liver disease, blood coagulation can be seriously affected. Portal hypertension, vascular abnormalities and/or a dysbalance in coagulation factors may result in bleeding disorders or in the development of thrombosis. Fibrinogen is the main protein involved in clot formation and wound healing. The aim of this work was to analyse the glycosylation pattern of the isolated fibrinogen molecules by lectin-based protein microarray, together with the carbonylation pattern of the individual fibrinogen chains, possible changes in the molecular secondary and tertiary structure and reactivity with the insulin-like growth factor-binding protein 1 (IGFBP-1) in patients with cirrhosis. The results pointed to an increase in several carbohydrate moieties: tri/tetra-antennary structures, Gal beta-1,4 GlcNAc, terminal alpha-2,3 Sia and alpha-1,3 Man, and a decrease in core alpha-1,6 Fuc and bi-antennary galactosylated N-glycans with bisecting GlcNAc. Fibrinogen A alpha chain was the most susceptible to carbonylation, followed by the B beta chain. Cirrhosis induced additional protein carbonylation, mostly on the alpha chain. Spectrofluorimetry and CD spectrometry detected reduction in the alpha-helix content, protein unfolding and/or appearance of modified amino acid residues in cirrhosis. The amount of complexes which fibrinogen forms with IGFBP-1, another factor involved in wound healing was significantly greater in patients with cirrhosis than in healthy individuals. A more detailed knowledge of individual molecules in coagulation process may contribute to deeper understanding of coagulopathies and the results of this study offer additional information on the possible mechanisms involved in impaired coagulation due to cirrhosis.",
publisher = "Pergamon-Elsevier Science Ltd, Oxford",
journal = "Thrombosis Research",
title = "Structural changes of fibrinogen as a consequence of cirrhosis",
volume = "166",
pages = "43-49",
doi = "10.1016/j.thromres.2018.04.005"
}
Gligorijević, N., Minić, S. L., Krizakova, M., Katrlik, J.,& Nedić, O. (2018). Structural changes of fibrinogen as a consequence of cirrhosis.
Thrombosis Research
Pergamon-Elsevier Science Ltd, Oxford., 166, 43-49.
https://doi.org/10.1016/j.thromres.2018.04.005
Gligorijević N, Minić SL, Krizakova M, Katrlik J, Nedić O. Structural changes of fibrinogen as a consequence of cirrhosis. Thrombosis Research. 2018;166:43-49
Gligorijević Nikola, Minić Simeon L., Krizakova Martina, Katrlik Jaroslav, Nedić Olgica, "Structural changes of fibrinogen as a consequence of cirrhosis" Thrombosis Research, 166 (2018):43-49,
https://doi.org/10.1016/j.thromres.2018.04.005 .
4
4
4

Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin

Minić, Simeon L.; Stanić-Vučinić, Dragana; Radomirović, Mirjana Ž.; Radibratović, Milica; Milčić, Miloš K.; Nikolić, Milan; Ćirković-Veličković, Tanja

(Elsevier, 2017)

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Radomirović, Mirjana Ž.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3035
AB  - Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (Ka = 2 × 106 M−1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin.
PB  - Elsevier
T2  - Food Chemistry
T1  - Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin
VL  - 239
SP  - 1090
EP  - 1099
DO  - 10.1016/j.foodchem.2017.07.066
ER  - 
@article{
author = "Minić, Simeon L. and Stanić-Vučinić, Dragana and Radomirović, Mirjana Ž. and Radibratović, Milica and Milčić, Miloš K. and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3035",
abstract = "Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (Ka = 2 × 106 M−1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin.",
publisher = "Elsevier",
journal = "Food Chemistry",
title = "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin",
volume = "239",
pages = "1090-1099",
doi = "10.1016/j.foodchem.2017.07.066"
}
Minić, S. L., Stanić-Vučinić, D., Radomirović, M. Ž., Radibratović, M., Milčić, M. K., Nikolić, M.,& Ćirković-Veličković, T. (2017). Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin.
Food Chemistry
Elsevier., 239, 1090-1099.
https://doi.org/10.1016/j.foodchem.2017.07.066
Minić SL, Stanić-Vučinić D, Radomirović MŽ, Radibratović M, Milčić MK, Nikolić M, Ćirković-Veličković T. Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. Food Chemistry. 2017;239:1090-1099
Minić Simeon L., Stanić-Vučinić Dragana, Radomirović Mirjana Ž., Radibratović Milica, Milčić Miloš K., Nikolić Milan, Ćirković-Veličković Tanja, "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin" Food Chemistry, 239 (2017):1090-1099,
https://doi.org/10.1016/j.foodchem.2017.07.066 .
18
19

Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin

Minić, Simeon L.; Radomirović, Mirjana Ž.; Radibratović, Milica; Milčić, Miloš K.; Stanić-Vučinić, Dragana; Nikolić, Milan; Ćirković-Veličković, Tanja

(Wiley, Hoboken, 2017)

TY  - CONF
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2408
AB  - Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (Ka = 2 × 106 M−1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin.
PB  - Wiley, Hoboken
C3  - FEBS Journal / Federation of European of Biochemical Societies
T1  - Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin
VL  - 284
SP  - 189
EP  - 190
DO  - 10.1016/j.foodchem.2017.07.066
ER  - 
@conference{
author = "Minić, Simeon L. and Radomirović, Mirjana Ž. and Radibratović, Milica and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2017",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2408",
abstract = "Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin, the main protein of the microalga Spirulina, with numerous proven health-related benefits. We examined binding of PCB to bovine serum albumin (BSA) and how it affects protein and ligand stability. Protein fluorescence quenching and microscale thermophoresis demonstrated high-affinity binding (Ka = 2 × 106 M−1). Spectroscopic titration with molecular docking analysis revealed two binding sites on BSA, at the inter-domain cleft and at subdomain IB, while CD spectroscopy indicated stereo-selective binding of the P conformer of the pigment to the protein. The PCB protein complex showed increased thermal stability. Although complex formation partly masked the antioxidant properties of PCB and BSA, a mutually protective effect against free radical-induced oxidation was found. BSA could be suitable for delivery of PCB as a food colorant or bioactive component. Our results also highlight subtle differences between PCB binding to bovine vs. human serum albumin.",
publisher = "Wiley, Hoboken",
journal = "FEBS Journal / Federation of European of Biochemical Societies",
title = "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin",
volume = "284",
pages = "189-190",
doi = "10.1016/j.foodchem.2017.07.066"
}
Minić, S. L., Radomirović, M. Ž., Radibratović, M., Milčić, M. K., Stanić-Vučinić, D., Nikolić, M.,& Ćirković-Veličković, T. (2017). Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin.
FEBS Journal / Federation of European of Biochemical Societies
Wiley, Hoboken., 284, 189-190.
https://doi.org/10.1016/j.foodchem.2017.07.066
Minić SL, Radomirović MŽ, Radibratović M, Milčić MK, Stanić-Vučinić D, Nikolić M, Ćirković-Veličković T. Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin. FEBS Journal / Federation of European of Biochemical Societies. 2017;284:189-190
Minić Simeon L., Radomirović Mirjana Ž., Radibratović Milica, Milčić Miloš K., Stanić-Vučinić Dragana, Nikolić Milan, Ćirković-Veličković Tanja, "Characterization and effects of binding of food-derived bioactive phycocyanobilin to bovine serum albumin" FEBS Journal / Federation of European of Biochemical Societies, 284 (2017):189-190,
https://doi.org/10.1016/j.foodchem.2017.07.066 .
18
19

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

Peruško, Marija; Al-Hanish, Ayah; Mihailović-Vesić, Jelena; Minić, Simeon L.; Trifunović, Sara; Prodić, Ivana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2017)

TY  - BOOK
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  - http://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
ER  - 
@book{
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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3027",
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"
}
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.
Food Chemistry
Elsevier Sci Ltd, Oxford..
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. Food Chemistry. 2017;
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" Food Chemistry (2017)

Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction

Peruško, Marija; Al-Hanish, Ayah; Mihailović-Vesić, Jelena; Minić, Simeon L.; Trifunović, Sara; Prodić, Ivana; Ćirković-Veličković, Tanja

(Elsevier Sci Ltd, Oxford, 2017)

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  - http://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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2456",
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.
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. Food Chemistry. 2017;232:744-752
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" Food Chemistry, 232 (2017):744-752,
https://doi.org/10.1016/j.foodchem.2017.04.074 .
21
19
21

Struktura, biološka aktivnost i interakcije sa proteinama fikocijanobilina i hromopeptida C-fikocijanina iz cijanobakterije Arthrospira platensis

Minić, Simeon L.

(Универзитет у Београду, Хемијски факултет, 2017)

TY  - BOOK
AU  - Minić, Simeon L.
PY  - 2017
UR  - http://eteze.bg.ac.rs/application/showtheses?thesesId=5609
UR  - https://fedorabg.bg.ac.rs/fedora/get/o:17149/bdef:Content/download
UR  - http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=49837327
UR  - http://nardus.mpn.gov.rs/123456789/9238
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2752
AB  - Arthrospira (Spirulina), fotosintetska filamentozna cijanobakterija, koristi se u ishrani čovjeka od davnina. To je jedan od najbogatijih izvora proteina i esencijalnih amino kiselina, kao i izvanredan izvor vitamina, makro- i mikro-elemenata, esencijalnih masnih kiselina, pigmenata, glikolipida i polisaharida. C-fikocijanin (C-PC), najzastupljeniji protein u Spirulini, je u vodi rastvoran heterodimerni molekul koji se odlikuje intezivnom fluorescencijom. Njegova plava boja potiče od kovalentno vezane (tioetarskom vezom) tetrapirolne hromofore fikocijanobilina. Jedan molekul PCB-a je vezan za α subjedinicu preko cisteinskog ostatka 84, dok β subjedinica vezuje dva molekula hromofore preko cisteinskih ostataka 82 i 153. Brojne studije su pokazale da C-PC ima značajne antoksidativne, anti-inflamatorne, imunomodulatorne i antikancerogene efekte. Štaviše, PCB per se ispoljava različite biološke aktivnosti koje mogu poboljšati zdravlje ljudi. U literaturi ne postoje podaci o strukturi i bioaktivnosti digestijom oslobođenih peptida sa vezanom hromoforom (hromopeptida), kao ni informacije o vezivanju PCB-a za humani (HSA) i goveđi (BSA) serum albumin, glavne proteine plazme i model sisteme za proučavanje protein-ligand interakcija.Prvi dio ove doktorske disertacije imao je za zadatak ispitivanje digestibilnosti (C-PC-a) pepsinom, kao i određivanje strukture i ispitivanje bioaktivnih svojstava hromopeptida dobijenih nakon digestije C-PC-a, izolovanog i prečiščenog iz komercijalnog praha Arthrospira platensis. SDS-PAGE pod redukujućim uslovima je pokazala da se hromoprotein brzo digestuje pepsinom u simuliranoj želudačnoj tečnosti. HPLC analiza digesta je pokazala postojanje pet dominantnih hromopeptidnih frakcija. Struktura oslobođenih hromopeptida je određena primjenom tandemske masene spektrometrije i peptidi, sa varijacijom u veličini od 2 do 13 aminokiselinska ostatka, su identifikovani u obje subjedinice C-PC-a. Utvrđeno je da sve hromopeptidne frakcije ispoljavaju odličnu antioksidativnu (ORAC esej i test ukupne redukujuće moći) i Cu2+-helirajuću aktivnost (studija gašenja fluorescencije), kao i značajne citotoksične efekte (MTT esej vijabilnosti) na ćelijskim linijama humanog cervikalnog adenokarcinoma i epitelnog kancera kolona. Zaključeno je da digestija pepsinom oslobađa biološki aktivne hromopeptide iz C-PC-a, čija je aktivnost u najvećoj mjeri zasnovana na njihovom antioksidativnom potencijalu.U drugom dijelu ove disertacije, najpre je okarakterisano vezivanje (prethodno izolovanog) PCB-a za HSA, a zatim je ispitan uticaj liganda na stabilnost proteina...
AB  - Arthrospira (Spirulina), photosynthetic, filamentous cyanobacteria, has been used as food for centuries. It is one of the the richest known natural source of proteins and essential amino acids, excellent source of vitamins, macro- and micro-elements, pigments, essential fatty acids, glycolipids, and polysaccharides. C-phycocyanin (C-PC), the most abundant protein of Spirulina, is highly fluorescent and water-soluble heterodimeric protein. Its blue color arises from covalently attached (via tioether bond) tetrapyrrole chromophore phycocyanobilin (PCB). One PCB molecule is attached to α-subunit via Cys 84, while β-subunit binds two molecules of PCB via cysteines 82 and 153. Numerous studies have shown C-PC exhibit significant antioxidative and free radical-scavenging properties, anti-inflammatory, immunomodulatory and anti-cancer effects. Furthermore, PCB itself exhibits various strong health-promoting activities. There are no literature data evaluating structure and bioactivities of peptides with bound chromophore (chromopeptides) released in C-PC digest, nor information on the PCB binding to HSA and BSA, major plasma proteins and model systems for studying protein-ligand interactions.First part of this thesis examined the structures and bioactivities of chromopeptides obtained by pepsin digestion of C-PC, isolated from commercial Arthrospira platensis powder. SDS-PAGE under reducing conditions has shown that chromoprotein is rapidly digested by pepsin in simulated gastric fluid. HPLC analyses of digest revealed five major chromopeptide fractions. 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-PC. It was shown that all chromopeptide fractions have excellent antioxidant (ORAC and reducing power test) and Cu2+-chelating (fluorescence quenching study) activities, and show significant cytotoxic effect (MTT viability assay) on human cervical adenocarcinoma and epithelial colonic cancer cell lines. Therefore, obtained results demonstrate that digestion by pepsin releases biologically active chromopeptides from C-phycocyanin whose activity is mostly related to the antioxidative potency provided by chromophore.In the seacond part, binding of PCB to HSA was studied, as well as effects of ligand binding on protein stability. Based on a computational approach (molecular docking), we demonstrated two putative high-affinity binding pockets on HSA for PCB chromophore...
PB  - Универзитет у Београду, Хемијски факултет
T2  - Универзитет у Београду
T1  - Struktura, biološka aktivnost i interakcije sa proteinama fikocijanobilina i hromopeptida C-fikocijanina iz cijanobakterije Arthrospira platensis
ER  - 
@phdthesis{
author = "Minić, Simeon L.",
year = "2017",
url = "http://eteze.bg.ac.rs/application/showtheses?thesesId=5609, https://fedorabg.bg.ac.rs/fedora/get/o:17149/bdef:Content/download, http://vbs.rs/scripts/cobiss?command=DISPLAY&base=70036&RID=49837327, http://nardus.mpn.gov.rs/123456789/9238, http://cherry.chem.bg.ac.rs/handle/123456789/2752",
abstract = "Arthrospira (Spirulina), fotosintetska filamentozna cijanobakterija, koristi se u ishrani čovjeka od davnina. To je jedan od najbogatijih izvora proteina i esencijalnih amino kiselina, kao i izvanredan izvor vitamina, makro- i mikro-elemenata, esencijalnih masnih kiselina, pigmenata, glikolipida i polisaharida. C-fikocijanin (C-PC), najzastupljeniji protein u Spirulini, je u vodi rastvoran heterodimerni molekul koji se odlikuje intezivnom fluorescencijom. Njegova plava boja potiče od kovalentno vezane (tioetarskom vezom) tetrapirolne hromofore fikocijanobilina. Jedan molekul PCB-a je vezan za α subjedinicu preko cisteinskog ostatka 84, dok β subjedinica vezuje dva molekula hromofore preko cisteinskih ostataka 82 i 153. Brojne studije su pokazale da C-PC ima značajne antoksidativne, anti-inflamatorne, imunomodulatorne i antikancerogene efekte. Štaviše, PCB per se ispoljava različite biološke aktivnosti koje mogu poboljšati zdravlje ljudi. U literaturi ne postoje podaci o strukturi i bioaktivnosti digestijom oslobođenih peptida sa vezanom hromoforom (hromopeptida), kao ni informacije o vezivanju PCB-a za humani (HSA) i goveđi (BSA) serum albumin, glavne proteine plazme i model sisteme za proučavanje protein-ligand interakcija.Prvi dio ove doktorske disertacije imao je za zadatak ispitivanje digestibilnosti (C-PC-a) pepsinom, kao i određivanje strukture i ispitivanje bioaktivnih svojstava hromopeptida dobijenih nakon digestije C-PC-a, izolovanog i prečiščenog iz komercijalnog praha Arthrospira platensis. SDS-PAGE pod redukujućim uslovima je pokazala da se hromoprotein brzo digestuje pepsinom u simuliranoj želudačnoj tečnosti. HPLC analiza digesta je pokazala postojanje pet dominantnih hromopeptidnih frakcija. Struktura oslobođenih hromopeptida je određena primjenom tandemske masene spektrometrije i peptidi, sa varijacijom u veličini od 2 do 13 aminokiselinska ostatka, su identifikovani u obje subjedinice C-PC-a. Utvrđeno je da sve hromopeptidne frakcije ispoljavaju odličnu antioksidativnu (ORAC esej i test ukupne redukujuće moći) i Cu2+-helirajuću aktivnost (studija gašenja fluorescencije), kao i značajne citotoksične efekte (MTT esej vijabilnosti) na ćelijskim linijama humanog cervikalnog adenokarcinoma i epitelnog kancera kolona. Zaključeno je da digestija pepsinom oslobađa biološki aktivne hromopeptide iz C-PC-a, čija je aktivnost u najvećoj mjeri zasnovana na njihovom antioksidativnom potencijalu.U drugom dijelu ove disertacije, najpre je okarakterisano vezivanje (prethodno izolovanog) PCB-a za HSA, a zatim je ispitan uticaj liganda na stabilnost proteina..., Arthrospira (Spirulina), photosynthetic, filamentous cyanobacteria, has been used as food for centuries. It is one of the the richest known natural source of proteins and essential amino acids, excellent source of vitamins, macro- and micro-elements, pigments, essential fatty acids, glycolipids, and polysaccharides. C-phycocyanin (C-PC), the most abundant protein of Spirulina, is highly fluorescent and water-soluble heterodimeric protein. Its blue color arises from covalently attached (via tioether bond) tetrapyrrole chromophore phycocyanobilin (PCB). One PCB molecule is attached to α-subunit via Cys 84, while β-subunit binds two molecules of PCB via cysteines 82 and 153. Numerous studies have shown C-PC exhibit significant antioxidative and free radical-scavenging properties, anti-inflammatory, immunomodulatory and anti-cancer effects. Furthermore, PCB itself exhibits various strong health-promoting activities. There are no literature data evaluating structure and bioactivities of peptides with bound chromophore (chromopeptides) released in C-PC digest, nor information on the PCB binding to HSA and BSA, major plasma proteins and model systems for studying protein-ligand interactions.First part of this thesis examined the structures and bioactivities of chromopeptides obtained by pepsin digestion of C-PC, isolated from commercial Arthrospira platensis powder. SDS-PAGE under reducing conditions has shown that chromoprotein is rapidly digested by pepsin in simulated gastric fluid. HPLC analyses of digest revealed five major chromopeptide fractions. 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-PC. It was shown that all chromopeptide fractions have excellent antioxidant (ORAC and reducing power test) and Cu2+-chelating (fluorescence quenching study) activities, and show significant cytotoxic effect (MTT viability assay) on human cervical adenocarcinoma and epithelial colonic cancer cell lines. Therefore, obtained results demonstrate that digestion by pepsin releases biologically active chromopeptides from C-phycocyanin whose activity is mostly related to the antioxidative potency provided by chromophore.In the seacond part, binding of PCB to HSA was studied, as well as effects of ligand binding on protein stability. Based on a computational approach (molecular docking), we demonstrated two putative high-affinity binding pockets on HSA for PCB chromophore...",
publisher = "Универзитет у Београду, Хемијски факултет",
journal = "Универзитет у Београду",
title = "Struktura, biološka aktivnost i interakcije sa proteinama fikocijanobilina i hromopeptida C-fikocijanina iz cijanobakterije Arthrospira platensis"
}
Minić, S. L. (2017). Struktura, biološka aktivnost i interakcije sa proteinama fikocijanobilina i hromopeptida C-fikocijanina iz cijanobakterije Arthrospira platensis.
Универзитет у Београду
Универзитет у Београду, Хемијски факултет..
Minić SL. Struktura, biološka aktivnost i interakcije sa proteinama fikocijanobilina i hromopeptida C-fikocijanina iz cijanobakterije Arthrospira platensis. Универзитет у Београду. 2017;
Minić Simeon L., "Struktura, biološka aktivnost i interakcije sa proteinama fikocijanobilina i hromopeptida C-fikocijanina iz cijanobakterije Arthrospira platensis" Универзитет у Београду (2017)

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

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

(Elsevier Sci Ltd, Oxford, 2016)

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

Supplementary material for the article: Radibratovic, M.; Minic, S.; Stanic-Vucinic, D.; Nikolic, M.; Milcic, M.; Velickovic, T. C. Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study. PLoS ONE 2016, 11 (12). https://doi.org/10.1371/journal.pone.0167973

Radibratović, Milica; Minić, Simeon L.; Stanić-Vučinić, Dragana; Nikolić, Milan; Milčić, Miloš K.; Ćirković-Veličković, Tanja

(Public Library Science, San Francisco, 2016)

TY  - BOOK
AU  - Radibratović, Milica
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/3614
PB  - Public Library Science, San Francisco
T2  - PLoS One / Public Library of Science
T1  - Supplementary material for the article: Radibratovic, M.; Minic, S.; Stanic-Vucinic, D.; Nikolic, M.; Milcic, M.; Velickovic, T. C. Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study. PLoS ONE 2016, 11 (12). https://doi.org/10.1371/journal.pone.0167973
ER  - 
@book{
author = "Radibratović, Milica and Minić, Simeon L. and Stanić-Vučinić, Dragana and Nikolić, Milan and Milčić, Miloš K. and Ćirković-Veličković, Tanja",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3614",
publisher = "Public Library Science, San Francisco",
journal = "PLoS One / Public Library of Science",
title = "Supplementary material for the article: Radibratovic, M.; Minic, S.; Stanic-Vucinic, D.; Nikolic, M.; Milcic, M.; Velickovic, T. C. Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study. PLoS ONE 2016, 11 (12). https://doi.org/10.1371/journal.pone.0167973"
}
Radibratović, M., Minić, S. L., Stanić-Vučinić, D., Nikolić, M., Milčić, M. K.,& Ćirković-Veličković, T. (2016). Supplementary material for the article: Radibratovic, M.; Minic, S.; Stanic-Vucinic, D.; Nikolic, M.; Milcic, M.; Velickovic, T. C. Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study. PLoS ONE 2016, 11 (12). https://doi.org/10.1371/journal.pone.0167973.
PLoS One / Public Library of Science
Public Library Science, San Francisco..
Radibratović M, Minić SL, Stanić-Vučinić D, Nikolić M, Milčić MK, Ćirković-Veličković T. Supplementary material for the article: Radibratovic, M.; Minic, S.; Stanic-Vucinic, D.; Nikolic, M.; Milcic, M.; Velickovic, T. C. Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study. PLoS ONE 2016, 11 (12). https://doi.org/10.1371/journal.pone.0167973. PLoS One / Public Library of Science. 2016;
Radibratović Milica, Minić Simeon L., Stanić-Vučinić Dragana, Nikolić Milan, Milčić Miloš K., Ćirković-Veličković Tanja, "Supplementary material for the article: Radibratovic, M.; Minic, S.; Stanic-Vucinic, D.; Nikolic, M.; Milcic, M.; Velickovic, T. C. Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study. PLoS ONE 2016, 11 (12). https://doi.org/10.1371/journal.pone.0167973" PLoS One / Public Library of Science (2016)

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

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

(Elsevier Sci Ltd, Oxford, 2016)

TY  - JOUR
AU  - Al-Hanish, Ayah
AU  - Stanić-Vučinić, Dragana
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Minić, Simeon L.
AU  - Stojadinović, Marija M.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/2299
AB  - Bovine alpha-lactalbumin (ALA) is an important Ca-binding protein of milk. Epigallocatechin-3-gallate (EGCG) is the major and the most biologically active catechin of green tea, which has the highest binding affinity to whey proteins due to galloyl functional group. In this study experimental and computational methods were used to investigate noncovalent interactions of EGCG and ALA. Binding affinity of EGCG for ALA, determined by fluorescence quenching analysis, was in the range described for complexes of EGCG and other dietary proteins, and lower than affinity of some phenolic compounds to ALA. Based on circular dichroism and Fourier transform infrared spectroscopy spectra, binding of EGCG change ALA conformation inducing alpha-helix to beta-structures transition. The isothermal titration calorimetry results suggest that the binding of EGCG to ALA is enthalpically favorable. The docking analysis shows that EGCG binds in the hydrophobic pocket at the entrance of cleft between alpha-helical and beta-sheetrich domains and includes residues of aromatic cluster II. Uptake of ALA by monocytes proceeds at a slower rate in the presence of EGCG suggesting that EGCG binding may impair uptake of ALA by antigen-presenting cells. ALA, being of low cost and widely available protein, can serve as suitable delivery system for EGCG, as well as for food fortification with this bioactive catechin. (C) 2016 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Hydrocolloids
T1  - Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate
VL  - 61
SP  - 241
EP  - 250
DO  - 10.1016/j.foodhyd.2016.05.012
ER  - 
@article{
author = "Al-Hanish, Ayah and Stanić-Vučinić, Dragana and Mihailović-Vesić, Jelena and Prodić, Ivana and Minić, Simeon L. and Stojadinović, Marija M. and Radibratović, Milica and Milčić, Miloš K. and Ćirković-Veličković, Tanja",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2299",
abstract = "Bovine alpha-lactalbumin (ALA) is an important Ca-binding protein of milk. Epigallocatechin-3-gallate (EGCG) is the major and the most biologically active catechin of green tea, which has the highest binding affinity to whey proteins due to galloyl functional group. In this study experimental and computational methods were used to investigate noncovalent interactions of EGCG and ALA. Binding affinity of EGCG for ALA, determined by fluorescence quenching analysis, was in the range described for complexes of EGCG and other dietary proteins, and lower than affinity of some phenolic compounds to ALA. Based on circular dichroism and Fourier transform infrared spectroscopy spectra, binding of EGCG change ALA conformation inducing alpha-helix to beta-structures transition. The isothermal titration calorimetry results suggest that the binding of EGCG to ALA is enthalpically favorable. The docking analysis shows that EGCG binds in the hydrophobic pocket at the entrance of cleft between alpha-helical and beta-sheetrich domains and includes residues of aromatic cluster II. Uptake of ALA by monocytes proceeds at a slower rate in the presence of EGCG suggesting that EGCG binding may impair uptake of ALA by antigen-presenting cells. ALA, being of low cost and widely available protein, can serve as suitable delivery system for EGCG, as well as for food fortification with this bioactive catechin. (C) 2016 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Hydrocolloids",
title = "Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate",
volume = "61",
pages = "241-250",
doi = "10.1016/j.foodhyd.2016.05.012"
}
Al-Hanish, A., Stanić-Vučinić, D., Mihailović-Vesić, J., Prodić, I., Minić, S. L., Stojadinović, M. M., Radibratović, M., Milčić, M. K.,& Ćirković-Veličković, T. (2016). Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate.
Food Hydrocolloids
Elsevier Sci Ltd, Oxford., 61, 241-250.
https://doi.org/10.1016/j.foodhyd.2016.05.012
Al-Hanish A, Stanić-Vučinić D, Mihailović-Vesić J, Prodić I, Minić SL, Stojadinović MM, Radibratović M, Milčić MK, Ćirković-Veličković T. Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate. Food Hydrocolloids. 2016;61:241-250
Al-Hanish Ayah, Stanić-Vučinić Dragana, Mihailović-Vesić Jelena, Prodić Ivana, Minić Simeon L., Stojadinović Marija M., Radibratović Milica, Milčić Miloš K., Ćirković-Veličković Tanja, "Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate" Food Hydrocolloids, 61 (2016):241-250,
https://doi.org/10.1016/j.foodhyd.2016.05.012 .
2
57
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56

Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin, a blue-colored biliprotein of microalga Spirulina

Minić, Simeon L.; Stanić-Vučinić, Dragana; Mihailović-Vesić, Jelena; Krstić-Ristivojević, Maja; Nikolić, Milan; Ćirković-Veličković, Tanja

(Elsevier Science Bv, Amsterdam, 2016)

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  - http://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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/2313",
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.
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. Journal of Proteomics. 2016;147:132-139
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" Journal of Proteomics, 147 (2016):132-139,
https://doi.org/10.1016/j.jprot.2016.03.043 .
7
20
16
18

Digestion by pepsin releases biologically active chromopeptides from C-phycocyanin, a blue-colored biliprotein of microalga Spirulina

Minić, Simeon L.; Stanić-Vučinić, Dragana; Mihailović-Vesić, Jelena; Krstić-Ristivojević, Maja; Nikolić, Milan; Ćirković-Veličković, Tanja

(Elsevier Science Bv, Amsterdam, 2016)

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  - http://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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3444",
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.
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. Journal of Proteomics. 2016;147:132-139
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" Journal of Proteomics, 147 (2016):132-139,
https://doi.org/10.1016/j.jprot.2016.03.043 .
7
20
16
18

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

Minić, Simeon L.; Stanić-Vučinić, Dragana; Mihailović-Vesić, Jelena; Krstić-Ristivojević, Maja; Nikolić, Milan; Ćirković-Veličković, Tanja

(Elsevier Science Bv, Amsterdam, 2016)

TY  - BOOK
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  - http://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
ER  - 
@book{
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",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/3445",
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"
}
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.
Journal of Proteomics
Elsevier Science Bv, Amsterdam..
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. Journal of Proteomics. 2016;
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" Journal of Proteomics (2016)

Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study

Radibratović, Milica; Minić, Simeon L.; Stanić-Vučinić, Dragana; Nikolić, Milan; Milčić, Miloš K.; Ćirković-Veličković, Tanja

(Public Library Science, San Francisco, 2016)

TY  - JOUR
AU  - Radibratović, Milica
AU  - Minić, Simeon L.
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/1948
AB  - Phycocyanobilin (PCB) binds with high affinity (2.2 x 10 6 M-1 at 25 degrees C) to human serum albumin (HSA) at sites located in IB and IIA subdomains. The aim of this study was to examine effects of PCB binding on protein conformation and stability. Using 300 ns molecular dynamics (MD) simulations, UV-VIS spectrophotometry, CD, FT-IR, spectrofluorimetry, thermal denaturation and susceptibility to trypsin digestion, we studied the effects of PCB binding on the stability and rigidity of HSA, as well as the conformational changes in PCB itself upon binding to the protein. MD simulation results demonstrated that HSA with PCB bound at any of the two sites showed greater rigidity and lower overall and individual domain flexibility compared to free HSA. Experimental data demonstrated an increase in the a-helical content of the protein and thermal and proteolytic stability upon ligand binding. PCB bound to HSA undergoes a conformational change to a more elongated conformation in the binding pockets of HSA. PCB binding to HSA stabilizes the structure of this flexible transport protein, making it more thermostable and resistant to proteolysis. The results from this work explain at molecular level, conformational changes and stabilization of HSA structure upon ligand binding. The resultant increased thermal and proteolytic stability of HSA may provide greater longevity to HSA in plasma.
PB  - Public Library Science, San Francisco
T2  - PLoS One / Public Library of Science
T1  - Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study
VL  - 11
IS  - 12
DO  - 10.1371/journal.pone.0167973
ER  - 
@article{
author = "Radibratović, Milica and Minić, Simeon L. and Stanić-Vučinić, Dragana and Nikolić, Milan and Milčić, Miloš K. and Ćirković-Veličković, Tanja",
year = "2016",
url = "http://cherry.chem.bg.ac.rs/handle/123456789/1948",
abstract = "Phycocyanobilin (PCB) binds with high affinity (2.2 x 10 6 M-1 at 25 degrees C) to human serum albumin (HSA) at sites located in IB and IIA subdomains. The aim of this study was to examine effects of PCB binding on protein conformation and stability. Using 300 ns molecular dynamics (MD) simulations, UV-VIS spectrophotometry, CD, FT-IR, spectrofluorimetry, thermal denaturation and susceptibility to trypsin digestion, we studied the effects of PCB binding on the stability and rigidity of HSA, as well as the conformational changes in PCB itself upon binding to the protein. MD simulation results demonstrated that HSA with PCB bound at any of the two sites showed greater rigidity and lower overall and individual domain flexibility compared to free HSA. Experimental data demonstrated an increase in the a-helical content of the protein and thermal and proteolytic stability upon ligand binding. PCB bound to HSA undergoes a conformational change to a more elongated conformation in the binding pockets of HSA. PCB binding to HSA stabilizes the structure of this flexible transport protein, making it more thermostable and resistant to proteolysis. The results from this work explain at molecular level, conformational changes and stabilization of HSA structure upon ligand binding. The resultant increased thermal and proteolytic stability of HSA may provide greater longevity to HSA in plasma.",
publisher = "Public Library Science, San Francisco",
journal = "PLoS One / Public Library of Science",
title = "Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study",
volume = "11",
number = "12",
doi = "10.1371/journal.pone.0167973"
}
Radibratović, M., Minić, S. L., Stanić-Vučinić, D., Nikolić, M., Milčić, M. K.,& Ćirković-Veličković, T. (2016). Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study.
PLoS One / Public Library of Science
Public Library Science, San Francisco., 11(12).
https://doi.org/10.1371/journal.pone.0167973
Radibratović M, Minić SL, Stanić-Vučinić D, Nikolić M, Milčić MK, Ćirković-Veličković T. Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study. PLoS One / Public Library of Science. 2016;11(12)
Radibratović Milica, Minić Simeon L., Stanić-Vučinić Dragana, Nikolić Milan, Milčić Miloš K., Ćirković-Veličković Tanja, "Stabilization of Human Serum Albumin by the Binding of Phycocyanobilin, a Bioactive Chromophore of Blue-Green Alga Spirulina: Molecular Dynamics and Experimental Study" PLoS One / Public Library of Science, 11, no. 12 (2016),
https://doi.org/10.1371/journal.pone.0167973 .
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