College of Life & Environment Science, Shanghai Normal University, PR China.
Crit Rev Food Sci Nutr. 2012;52(1):85-101. doi: 10.1080/10408398.2010.499017.
The interactions between polyphenols, especially flavonoids and plasma proteins, have attracted great interest among researchers. Few papers, however, have focused on the structure-affinity relationship of polyphenols on their affinities for plasma proteins. The aim of this review is to give an overview of the research reports on the characterization, influence on the bioactivity, and the structure-affinity relationship for studying the affinities between polyphenols and plasma proteins. The molecular properties that influence the affinities of polyphenols for plasma proteins are the following: 1) One or more hydroxyl groups in the B-ring (e.g., 3',4' dihydroxylated B ring catechol group) of flavonoids enhanced the binding affinities to proteins. However, the hydroxyl group in the C-ring will weaken the binding interaction. 2) The presence of an unsaturated 2,3-bond in conjugation with a 4-carbonyl group, characteristic of flavonols structure, has been associated with stronger binding affinity with plasma proteins; 3) The glycosylation of flavonoids decreases the affinities for plasma proteins by 1-3 orders of magnitude depending on the conjugation site and the class of sugar moiety; 4) The methylation of hydroxyl groups in flavonoids slightly enhanced the affinities for plasma proteins by 2-16 times; 5) The galloylated catechins have higher binding affinities for plasma proteins than do non-galloylated catechins and the pyrogallol-type catechins have higher affinities than do the catechol-type catechins. The affinity of the catechin with 2,3-trans structure was lower than those of the catechin with 2,3-cis structure; 6) The gallotannins with more gallol groups presented a much higher percentage of binding to plasma proteins. α-D-Gallotannin showed a greater affinity for plasma proteins than does the natural stereoisomer, β-D-gallotannin; 7) The binding degree of chlorogenic acid with only one caffeoyl group was lower than the binding degrees of caffeoyl quinic acids with more caffeoyl groups. The methylation of phenolic acid decreased the affinity for BSA.
多酚，尤其是类黄酮与血浆蛋白之间的相互作用引起了研究人员的极大兴趣。然而，很少有论文关注多酚与血浆蛋白亲和力的结构-亲和力关系。本文综述了多酚与血浆蛋白亲和力的研究报告，包括其特征、对生物活性的影响以及结构-亲和力关系。影响多酚与血浆蛋白亲和力的分子性质如下：1）黄酮类化合物 B 环上的一个或多个羟基（例如，3'，4' 二羟基 B 环邻苯二酚基团）增强了与蛋白质的结合亲和力。然而，C 环上的羟基会削弱结合相互作用。2）具有与 4-羰基共轭的不饱和 2,3-键的特征黄酮醇结构与与血浆蛋白更强的结合亲和力相关；3）根据结合位点和糖部分的类别，黄酮类化合物的糖基化使与血浆蛋白的亲和力降低 1-3 个数量级；4）黄酮类化合物中羟基的甲基化使与血浆蛋白的亲和力增强 2-16 倍；5）没食子酰化儿茶素比非没食子酰化儿茶素具有更高的与血浆蛋白的结合亲和力，而焦儿茶素型儿茶素比邻苯二酚型儿茶素具有更高的亲和力。2,3-反式结构的儿茶素的亲和力低于 2,3-顺式结构的儿茶素；6）具有更多没食子酰基的没食子单宁与血浆蛋白的结合率更高。α-D-没食子单宁比天然立体异构体β-D-没食子单宁对血浆蛋白具有更高的亲和力；7）只有一个咖啡酰基的绿原酸与 BSA 的结合程度低于具有更多咖啡酰基的咖啡酰奎宁酸。酚酸的甲基化降低了与 BSA 的亲和力。
