光谱法结合分子对接研究盐酸文拉法辛与牛血清白蛋白的相互作用

Study on the interaction of bovine serum albumin and venlafaxine hydrochloride by spectroscopy and molecular modeling method

为了解决盐酸文拉法辛荧光光谱与牛血清白蛋白(BSA)荧光光谱严重重叠的缺陷,在模拟人体生理条件下(p H 7.4 Tris-HCl缓冲液),以盐酸文拉法辛为荧光检测对象,BSA为猝灭剂,通过荧光光谱法研究了它们之间的相互作用。盐酸文拉法辛与BSA通过疏水作用力形成了一种稳定的复合物;由探针实验确定盐酸文拉法辛在BSA上的结合位点为位点Ⅰ;298K时结合常数为3.76×105L/mol,结合位点数约为1;Hill系数表明盐酸文拉法辛的药效受到温度的调控。利用分子对接技术模拟研究了二者的相互作用,其结果与光谱法获得的结果一致。

In the presence of simulating physiological systems, the interactionbetween BSA and venlafaxine hydrochloride （VH）was investigated by UV absorption spectroscopy, fluorescencespectroscopy and molecular modeling method. The results showed that the stable complex of VH - BSA was formed, the number of binding sites （n） in this binary system was approximately 1 and the binding constant （ Kb ） was 3.76× 10^5 L/tool at 298K. The results also confirmed that the binding power betweenVH and BSA was mainly hydrophobic power and the primary binding site was located at siteI in subdomain II A of BSA. Meanwhile, the value of Hill, s coefficients indicated that the pharmacodynamic effect of VH was affected by the temperature.