荧光光谱法研究虎杖苷与牛血清白蛋白的相互作用  

Study on the Interaction of Bovine Serum Albumin with Polydatin by Fluorescence Spectroscopy

作　　者：尚永辉[1,2] 杨格格[1] 胡文婷[1] 杨婷[1] 李进[1] 

机构地区：[1]咸阳师范学院化学与化工学院,陕西省咸阳市文林路712000 [2]西北大学分析科学研究所,西安市710069

出　　处：《光谱实验室》2010年第4期1273-1276,共4页Chinese Journal of Spectroscopy Laboratory

基　　金：国家自然科学基金(20975081);西北大学研究生交叉学科资助项目(07YJC09);咸阳师范学院专项科研基金项目(08XSYK218);咸阳师范学院大学生科研训练计划项目(08059)

摘　　要：在不同温度下,采用荧光光谱,紫外-可见吸收光谱研究了虎杖苷与牛血清白蛋白(BSA)的相互作用。虎杖苷对BSA的荧光有较强的猝灭作用。根据292K和311K时虎杖苷对BSA的荧光猝灭作用,利用Stern-Volmer方程及双倒数方程处理实验数据,表明虎杖苷对BSA的荧光猝灭作用属于动态猝灭过程,根据Foerster非辐射能量转移理论计算出了虎杖苷与BSA间的结合距离r=3.61nm,结合常数(Kb)分别为5.189×105L·mol-1(292K),1.382×105L·mol-1(311K)及对应温度下的热力学参数。实验结果表明二者主要靠疏水作用力结合,采用同步荧光光谱探讨了虎杖苷对BSA构象的影响。The binding reaction of polydatin with bovine serum albumin was studied at 292K and 311K by fluorescence and UV-Vis absorption spectroscopy.It was shown that polydatin has a strong ability of quenching the fluorescence of BSA.The Stern-Volmer curve and double logarithm equation of the fluorescence quenching of BSA by polydatin indicated that the quenching mechanism of polydatin to BSA was a dynamic quenching.According to the Foerster＇s theory of non-radiation energy transfer,the binding distances （r） was 3.61nm（292K）,the binding constants （Kb） were 5.189×105L·mol-1（292K）,1.382×105L·mol-1（311K）,respectively.The thermodynamic parameters showed that the interaction of polydatin and BSA was mainly driven by hydrophobic force.Synchronous spectrum was used to investigate the conformational changes of BSA.

关 键 词：虎杖苷 牛血清白蛋白 荧光光谱 

分 类 号：O657.32[理学—分析化学]