荧光光谱法研究葛根素与牛血清白蛋白的相互作用  

Study on interaction between bovine serum albumin and puerarin by fluorescence spectroscopy

作　　者：尚永辉[1,2] 李进[1] 杨婷[1] 孙家娟[1] 

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

出　　处：《分析仪器》2010年第2期52-55,共4页Analytical Instrumentation

基　　金：西北大学研究生交叉学科资助项目(07YJC09);陕西省教育厅基金项目(06JK164);咸阳师范学院专项科研基金项目(05XSYK105);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,采用荧光猝灭光谱法和同步荧光光谱法研究了葛根素与牛血清白蛋白(BSA)相互作用的光谱学行为。根据在292K和311K温度下葛根素对BSA的荧光猝灭作用,利用Stern-Volmer方程及双倒数方程对实验数据进行处理,结果表明葛根素对BSA的荧光猝灭作用属于静态猝灭过程。根据Frster非辐射能量转移理论计算出了葛根素与BSA间的结合距离r=2.84nm,结合常数(Kb)分别为1.334×105mol/L(292K)和4.513×105mol/L(311K)。热力学数据表明,二者主要靠静电引力结合。采用同步荧光光谱法分析了葛根素对BSA构象的影响。The binding reaction of purearin with bovine serum albumin （BSA） was studied under different tem- peratures （292K and 311K） by using fluorescence quenching spectra and synchronous fluorescence spectra. It was showed that puerarin had a quenching effect on the fluorescence of BSA. The experimental data was treated with Stern-Volmer equation and double-reciprocal equation. The results showed that the quenching effect of puerarin on the fluorescence of BSA was static quenching. According to F6rster theory of non-radiation energy intransfer, the binding distance between puerarin and BSA was calculated to be 2.84nm, and the binding constants （Kb） to be 1. 334×10^5L/mol（292K）, and 4. 513×10^5L/mol（311K）,respectively. The thermodynamic parameters showed that the interaction between puerarinn and BSA was mainly driven by electrostatic force. The infuence of puerarin on the conformation of BSA was investigated with synchronous spectra.

关 键 词：葛根素 牛血清白蛋白 荧光光谱法 

分 类 号：R285[医药卫生—中药学]