Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 62, Issue 17, Pages 3768-3775Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf500246m
Keywords
polyphenol; tea; tannin-protein interaction; molecular modeling; phenylbutazone; tolbutamide
Funding
- USDA [58-1932-5-534]
- NIDDK [R15DK069285]
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The principal green tea polyphenol, (-)-epigallocatechin-3-O-gallate (EGCg), may provide chemoprotection against conditions ranging from cardiovascular disease to cancer. Binding to plasma proteins stabilizes EGCg during its transport to targeted tissues. This study explored the details EGCg binding to bovine serum albumin. Both fluorescence lifetime and intensity data showed that the hydrophobic pocket between subdomains IIA and IIIA is the binding site for EGCg. Fluorescence and circular dichroism were used to establish the roles of the flavan-3-ol and galloyl moieties of the EGCg in binding and to demonstrate a binding-dependent conformational change in the protein. Competitive binding experiments confirmed the location of binding, and molecular modeling identified protein residues that play key roles in the interaction. This model of EGCg-BSA interactions improves the understanding of the likely physiological fate of this green tea-derived bioactive polyphenol.
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