荧光光谱法研究淫羊藿苷和淫羊藿次苷Ⅰ与牛血清白蛋白的相互作用(英文)  

Interactions of Icariin and IcarisideⅠ with Bovine Serum Albumin Analyzed by Fluorescence Spectroscopy

作　　者：要晓静[1] 赵伟[1] 阚鸿[1] 刘忠英[1] 

机构地区：[1]吉林大学药学院,长春130000

出　　处：《中国生物化学与分子生物学报》2012年第7期666-670,共5页Chinese Journal of Biochemistry and Molecular Biology

基　　金：Supported by National Natural Science Foundation of China(No.20953001)~~

摘　　要：在模拟生理条件下应用荧光光谱学方法分别研究了淫羊藿苷和淫羊藿次苷Ⅰ与牛血清白蛋白(BSA)间的结合作用.根据荧光强度数据,计算出了结合常数KA,结合位点数n和热力学参数(△G,△H和△S).实验结果表明,淫羊藿苷和淫羊藿次苷Ⅰ都能显著猝灭BSA的内源荧光,猝灭机制均为形成基态复合物的单一静态猝灭过程.不同温度下(17℃,27℃,37℃)得到的KA和n值,表明淫羊藿次苷Ⅰ与BSA的结合强于淫羊藿苷.从得到的热力学参数判断,淫羊藿苷与BSA间的主要作用力是氢键作用和范德华力,而疏水作用和静电引力在淫羊藿次苷Ⅰ与BSA形成复合物过程中起主导作用.而且同步荧光光谱显示,淫羊藿苷和淫羊藿次苷Ⅰ与BSA的结合导致BSA构象发生了变化.The interactions of icariin and icarisideⅠ with bovine serum albumin（BSA） under simulated physiologic conditions was investigated by fluorescence spectroscopy.The binding constants（KA）,number of binding sites（n） of icariin / icarisideⅠ with BSA,and other thermodynamic parameters（△G,△H and △S） were calculated.The experimental results showed that both icariin and icarisideⅠ significantly quenched the intrinsic fluorescence of BSA through a single static process by forming a ground state complex.The values of KA and n at different temperatures（17 ℃,27 ℃,37 ℃） indicated that icarisideⅠ bound BSA stronger than icariin could.The thermodynamic measures suggested that the forces for icariin to bind BSA were mainly the hydrogen bonding and van der Waals force,whereas the hydrophobic and electrostatic interactions were the leading forces to form icarisideⅠ and BSA complex.In addition,conformational changes of BSA were observed from the synchronous fluorescence spectra upon the binding of icariin and icariside I.

关 键 词：淫羊藿苷 淫羊藿次苷Ⅰ 牛血清白蛋白 相互作用 荧光光谱法 

分 类 号：Q51[生物学—生物化学]