蒽醌及黄酮类化合物与牛血清白蛋白结合的反应研究  

Binding of Anthraquinones and Flavonoids to Bovine Serum Albumin

作　　者：张保林[1] 王文清[1] 袁荣尧[1] 

机构地区：[1]北京大学技术物理系

出　　处：《化学学报》1994年第12期1208-1212,共5页Acta Chimica Sinica

基　　金：国家自然科学基金资助的课题

摘　　要：用离心超过滤法测定了十四种不同结构的蒽醌及黄酮类化合物与牛血清白蛋白(BSA)的结合常数和结合部位数目.发现这些化合物与BSA的结合能力随其脂溶性增加而增大,龙胆苦苷不与BSA结合.研究了L-色氨酸、油酸与大黄素对BSA的竞争结合反应.结果表明L—色氨酸和大黄素拥有一个相同的强结合部位,可以发生1:1置换反应.低浓度油酸存在下使大黄素等同的6个结合部位区分为两类:n1=2,n2=4,总结合部位数目不变,但结合常数显著减小,油酸浓度足够大时,大黄素完全不与BSA结合,测得大黄素与BSA结合的△H≈0.根据上述结果,对蒽醌及黄酮类化合物与BSA结合反应机理进行了初步探讨.Binding of 14 kinds hydrophobic compounds of anthraquinones and flavonoids, which distribute extensively in many Chinese herbal medicine, to bovine serum albumin (BSA) were studied using centrifugal ultrifiltration. The binding data was analyzed according to Scatchard model, and the binding constants and the binding site number were obtained, respectively. The results show that the affinity of these compounds to BSA increases as their hydrophobicity higher except gertiopicrin. Competitive binding studies indicate that L-tryptephan and emodin share one primary site, addition of excess L-Trp will result in the displacement of one molar equivalence emodin. In the presence of low concentration oleate, the six homogeneous sites of emodin are distinguished into two classes: n1=2, n2=4, the total number of binding sites remains unchangable while the binding constants decrease. When the oleate concentration is high enough, emodin will thoroughly not bind to BSA. The temperature dependence of the binding constants reveals that the binding enthalpy is nearly zero. On this basis, the mechanism of the binding reaction was discussed in brief.

关 键 词：蒽醌 黄酮类化合物 牛血清白蛋白 结合常数 

分 类 号：O625.463[理学—有机化学]