Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate
Samo za registrovane korisnike
2016
Autori
Al-Hanish, AyahStanić-Vučinić, Dragana
Mihailović-Vesić, Jelena
Prodić, Ivana
Minić, Simeon L.
Stojadinović, Marija M.
Radibratović, Milica
Milčić, Miloš K.
Ćirković-Veličković, Tanja
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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-he...lical 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.
Ključne reči:
alpha-Lactalbumin / Epigallocatechin-3-gallate / Noncovalent interactions / Fluorescence quenching / Molecular docking / Monocyte uptakeIzvor:
Food Hydrocolloids, 2016, 61, 241-250Izdavač:
- Elsevier Sci Ltd, Oxford
Finansiranje / projekti:
- Molekularne osobine i modifikacije nekih respiratornih i nutritivnih alergena (RS-MESTD-Basic Research (BR or ON)-172024)
- Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-FP7-256716)
Napomena:
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3585
DOI: 10.1016/j.foodhyd.2016.05.012
ISSN: 0268-005X
WoS: 000382253400027
Scopus: 2-s2.0-84969961344
Institucija/grupa
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Al-Hanish, Ayah AU - Stanić-Vučinić, Dragana AU - Mihailović-Vesić, Jelena AU - Prodić, Ivana AU - Minić, Simeon L. AU - Stojadinović, Marija M. AU - Radibratović, Milica AU - Milčić, Miloš K. AU - Ćirković-Veličković, Tanja PY - 2016 UR - https://cherry.chem.bg.ac.rs/handle/123456789/2299 AB - Bovine alpha-lactalbumin (ALA) is an important Ca-binding protein of milk. Epigallocatechin-3-gallate (EGCG) is the major and the most biologically active catechin of green tea, which has the highest binding affinity to whey proteins due to galloyl functional group. In this study experimental and computational methods were used to investigate noncovalent interactions of EGCG and ALA. Binding affinity of EGCG for ALA, determined by fluorescence quenching analysis, was in the range described for complexes of EGCG and other dietary proteins, and lower than affinity of some phenolic compounds to ALA. Based on circular dichroism and Fourier transform infrared spectroscopy spectra, binding of EGCG change ALA conformation inducing alpha-helix to beta-structures transition. The isothermal titration calorimetry results suggest that the binding of EGCG to ALA is enthalpically favorable. The docking analysis shows that EGCG binds in the hydrophobic pocket at the entrance of cleft between alpha-helical and beta-sheetrich domains and includes residues of aromatic cluster II. Uptake of ALA by monocytes proceeds at a slower rate in the presence of EGCG suggesting that EGCG binding may impair uptake of ALA by antigen-presenting cells. ALA, being of low cost and widely available protein, can serve as suitable delivery system for EGCG, as well as for food fortification with this bioactive catechin. (C) 2016 Elsevier Ltd. All rights reserved. PB - Elsevier Sci Ltd, Oxford T2 - Food Hydrocolloids T1 - Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate VL - 61 SP - 241 EP - 250 DO - 10.1016/j.foodhyd.2016.05.012 ER -
@article{ author = "Al-Hanish, Ayah and Stanić-Vučinić, Dragana and Mihailović-Vesić, Jelena and Prodić, Ivana and Minić, Simeon L. and Stojadinović, Marija M. and Radibratović, Milica and Milčić, Miloš K. and Ćirković-Veličković, Tanja", year = "2016", abstract = "Bovine alpha-lactalbumin (ALA) is an important Ca-binding protein of milk. Epigallocatechin-3-gallate (EGCG) is the major and the most biologically active catechin of green tea, which has the highest binding affinity to whey proteins due to galloyl functional group. In this study experimental and computational methods were used to investigate noncovalent interactions of EGCG and ALA. Binding affinity of EGCG for ALA, determined by fluorescence quenching analysis, was in the range described for complexes of EGCG and other dietary proteins, and lower than affinity of some phenolic compounds to ALA. Based on circular dichroism and Fourier transform infrared spectroscopy spectra, binding of EGCG change ALA conformation inducing alpha-helix to beta-structures transition. The isothermal titration calorimetry results suggest that the binding of EGCG to ALA is enthalpically favorable. The docking analysis shows that EGCG binds in the hydrophobic pocket at the entrance of cleft between alpha-helical and beta-sheetrich domains and includes residues of aromatic cluster II. Uptake of ALA by monocytes proceeds at a slower rate in the presence of EGCG suggesting that EGCG binding may impair uptake of ALA by antigen-presenting cells. ALA, being of low cost and widely available protein, can serve as suitable delivery system for EGCG, as well as for food fortification with this bioactive catechin. (C) 2016 Elsevier Ltd. All rights reserved.", publisher = "Elsevier Sci Ltd, Oxford", journal = "Food Hydrocolloids", title = "Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate", volume = "61", pages = "241-250", doi = "10.1016/j.foodhyd.2016.05.012" }
Al-Hanish, A., Stanić-Vučinić, D., Mihailović-Vesić, J., Prodić, I., Minić, S. L., Stojadinović, M. M., Radibratović, M., Milčić, M. K.,& Ćirković-Veličković, T.. (2016). Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate. in Food Hydrocolloids Elsevier Sci Ltd, Oxford., 61, 241-250. https://doi.org/10.1016/j.foodhyd.2016.05.012
Al-Hanish A, Stanić-Vučinić D, Mihailović-Vesić J, Prodić I, Minić SL, Stojadinović MM, Radibratović M, Milčić MK, Ćirković-Veličković T. Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate. in Food Hydrocolloids. 2016;61:241-250. doi:10.1016/j.foodhyd.2016.05.012 .
Al-Hanish, Ayah, Stanić-Vučinić, Dragana, Mihailović-Vesić, Jelena, Prodić, Ivana, Minić, Simeon L., Stojadinović, Marija M., Radibratović, Milica, Milčić, Miloš K., Ćirković-Veličković, Tanja, "Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate" in Food Hydrocolloids, 61 (2016):241-250, https://doi.org/10.1016/j.foodhyd.2016.05.012 . .