Resveratrol, Genistein, and Curcumin Bind Bovine Serum Albumin

被引：360

作者：

Bourassa, P. ^{[1
]}

Kanakis, C. D. ^{[2
]}

Tarantilis, P. ^{[2
]}

Pollissiou, M. G. ^{[2
]}

Tajmir-Riahi, H. A. ^{[1
]}

机构：

[1] Univ Quebec Trois Rivieres, Dept Chim Biol, Trois Rivieres, PQ G9A 5H7, Canada

[2] Agr Univ Athens, Dept Sci, Chem Lab, Athens 11855, Greece

来源：

JOURNAL OF PHYSICAL CHEMISTRY B | 2010年 / 114卷 / 09期

基金：

加拿大自然科学与工程研究理事会;

关键词：

CIRCULAR-DICHROISM SPECTRA; SECONDARY STRUCTURE; CONFORMATIONAL-CHANGES; TRANS-RESVERATROL; SWISS-MODEL; ACID; COMPLEXATION; SPECTROSCOPY; STABILITY; DRUGS;

D O I：

10.1021/jp9115996

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

We report the complexation of bovine serum albumin (BSA) with resveratrol, genistein, and curcumin, at physiological conditions, using constant protein concentration and various polyphenol contents. FTIR, CD, and fluorescence spectroscopic methods were used to analyze the ligand binding mode, the binding constant, and the effects of complexation on BSA stability and conformation. Structural analysis showed that polyphenols bind BSA via hydrophilic and hydrophobic interactions with the number of bound polyphenol (n) being 1.30 for resveratrol-BSA, 1.30 for genisten-BSA, and 1.0 for curcumin-BSA. The polyphenol-BSA binding constants were KRes-BSA = 2.52(+/-0.5) x 10(4) M-1, KGen-BSA = 1.26(+/-0.3) x 10(4) M-1, and KCur-BSA = 3.33(+/-0.8) x 10(4) M-1. Polyphenol binding altered BSA conformation with a major reduction of alpha-helix and an increase in beta-sheet and turn structures, indicating a partial protein unfolding.

引用

页码：3348 / 3354

页数：7

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