Département de Chimie-Biologie, Université du Québec à Trois-Rivières, C. P. 500, Trois-Rivières (Québec), G9A 5H7, Canada.
J Phys Chem B. 2010 Mar 11;114(9):3348-54. doi: 10.1021/jp9115996.
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 genistein-BSA, and 1.0 for curcumin-BSA. The polyphenol-BSA binding constants were K(Res-BSA) = 2.52(+/-0.5) x 10(4) M(-1), K(Gen-BSA) = 1.26(+/-0.3) x 10(4) M(-1), and K(Cur-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.
我们报告了牛血清白蛋白（BSA）与白藜芦醇、染料木黄酮和姜黄素在生理条件下的络合作用，使用恒定的蛋白质浓度和各种多酚含量。傅里叶变换红外光谱（FTIR）、圆二色光谱（CD）和荧光光谱方法用于分析配体结合模式、结合常数以及络合对 BSA 稳定性和构象的影响。结构分析表明，多酚通过亲水和疏水相互作用与 BSA 结合，与 BSA 结合的多酚数量（n）分别为白藜芦醇-BSA 中的 1.30、染料木黄酮-BSA 中的 1.30 和姜黄素-BSA 中的 1.0。多酚-BSA 结合常数为 K（Res-BSA）= 2.52(+/-0.5) x 10(4) M(-1)，K（Gen-BSA）= 1.26(+/-0.3) x 10(4) M(-1)，和 K（Cur-BSA）= 3.33(+/-0.8) x 10(4) M(-1)。多酚结合改变了 BSA 的构象，主要减少了α-螺旋结构，增加了β-折叠和转角结构，表明部分蛋白质展开。
