Noncovalent interactions of bovine α-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate
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- 作者：Ayah Al-Hanish1 ; Dragana Stanic-Vucinic1 ; Jelena Mihailovic ; Ivana Prodic ; Simeon Minic ; Marija Stojadinovic ; Milica Radibratovic ; Milos Milcic ; Tanja Cirkovic Velickovic ; tcirkov@chem.bg.ac.rs" class="auth_mail" title="E-mail the corresponding author
- 关键词：α-Lactalbumin ; Epigallocatechin-3-gallate ; Noncovalent interactions ; Fluorescence quenching ; Molecular docking ; Monocyte uptake
- 刊名：Food Hydrocolloids
- 出版年：2016
- 出版时间：December 2016
- 年：2016
- 卷：61
- 期：Complete
- 页码：241-250
- 全文大小：1174 K
文摘
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Whey protein α-lactalbumin interacts with the major green tea catechin, EGCG.
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Binding of EGCG results in α-helix to β-sheet transition in α-lactalbumin structure.
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EGCG binds in the hydrophobic pocket at the cleft between two domains.
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EGCG binding impairs α-lactalbumin uptake by monocytes.
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α-lactalbumin can serve as suitable delivery system of EGCG.
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