中文摘要：

运用荧光光谱法研究了抗癌药物白藜芦醇（resveratrol，Res）与人血清白蛋白（human serum albumin，HSA）的相互作用．结果显示，在生理条件下，HSA使Res的荧光最大发射峰发生明显蓝移，说明药物与蛋白间发生相互作用．平衡透析结果表明，Res在HSA上只有一个结合位点．Res对HSA的荧光猝灭是静态猝灭过程，药物与蛋白之间形成复合物，结合常数为7．43×10^5L／mol（298K），结合距离为3．50nm．8-苯胺基-1-萘磺酸（8-anilion-1-naphthalenesulfonic acid，ANS）结合研究及热力学分析结果表明Res结合在HSA的疏水腔内，疏水作用为主要结合力．

英文摘要：

The interaction of the anticancer drug resveratrol （Res） with human serum albumin （HSA） has been investigated by fluorescence spectroscopy. The fluorescence spectra show that the addition of HSA results in a distinct blue shift in the maximum emission peak of Res, which indicates that there is interaction between Res and HSA. Equilibrium dialysis results show that there is only one Res binding site on HSA. The fluorescence quenching of HSA induced by Res is static quenching procedure and a complex of Res and HSA may be formed. The binding constant is 7.43 × 10^5 L/mol^-1 at 298 K. The distance between Res and HSA is 3.50 nm. 8-Anilion-1-naphthalenesulfonic acid binding studies and thermodynamic analysis suggest that Res binds to the hydrophobic cavities of HSA, and hydrophobic interaction plays a major role in the binding of Res to HSA.