Interaction of β-Lactoglobulin with resveratrol and its biological implications
Interaction of β-Lactoglobulin with resveratrol and its biological implications
复制标题
DOI：
10.1021/bm700728k
复制
发表时间：
2008-01-01
影响因子：
6.2
通讯作者：
Subirade, Muriel
中科院分区：
文献类型：
--
作者：
Liang, Li;Tajmir-Riahi, H. A.;Subirade, Muriel
β-乳球蛋白（β-LG）是反刍动物乳中的主要乳清蛋白，对多种化合物具有高亲和力。白藜芦醇（3，5，4 '-三羟基芪）是一种天然多酚化合物，存在于葡萄和红葡萄酒中，具有许多与健康益处相关的生理作用。本文采用圆二色谱、荧光光谱和紫外-可见吸收光谱研究了白藜芦醇与β-LG的相互作用。白藜芦醇的自缔合可能发生在高浓度。白藜芦醇与β-LG相互作用形成1：1复合物。白藜芦醇与蛋白质表面结合，因为β-LG结合的多酚相对于75%乙醇处于较弱的疏水环境中。白藜芦醇-β-LG相互作用的结合常数在10（4）和10（6）M-1之间，通过蛋白质或多酚荧光测定。β-LG-白藜芦醇的相互作用可能会与多酚和蛋白质的自结合竞争。它对β-LG二级结构没有明显影响，但部分破坏三级结构。与β-LG的复合提供了白藜芦醇的光稳定性的轻微增加和其水溶性的显着增加。
beta-Lactoglobulin (beta-LG), the major whey protein in the milk of ruminants, has a high affinity for a wide range of compounds. Resveratrol (3,5,4'-trihydroxystilbene), a natural polyphenolic compound found in grapes and red wine, exhibits many physiological effects associated with health benefits. In this study, the interaction of resveratrol with beta-LG was investigated using circular dichroism, fluorescence and UV-vis absorbance. Self-association of resveratrol possibly occurs at high concentrations. Resveratrol interacts with beta-LG to form 1:1 complexes. Resveratrol is bound to the surface of the protein because beta-LG-bound polyphenol is in a weaker hydrophobic environment relative to 75% ethanol. The binding constant for the resveratrol-beta-LG interaction is between 10(4) and 10(6) M-1, as determined by protein or polyphenol fluorescence. The beta-LG-resveratrol interaction may compete with self-association of both the polyphenol and the protein. It has no apparent influence on beta-LG secondary structure but partially disrupts tertiary structure. Complexing with beta-LG provides a slight increase in the photostability of resveratrol and a significant increase in its hydrosolubility.