贝加因与牛血清白蛋白相互作用的分子光谱法研究(英文)  

Study of interaction between baicalein and bovine serum albumin by molecular spectrometry

作　　者：熊利敏[1,2,3] 宋胜梅[2,3] 张银堂[2] 徐茂田[1,2,3] 

机构地区：[1]中南大学化学与化工学院,湖南长沙410083 [2]商丘师范学院化学系,河南省纳米生物分析化学重点实验室培育基地,河南商丘476000 [3]郑州大学化学系,河南郑州450001

出　　处：《化学研究》2011年第1期9-13,共5页Chemical Research

基　　金：supported by the National Science Foundation of China(20775047 and 20905045)

摘　　要：利用荧光光谱和吸收光谱研究了贝加因与牛血清白蛋白(BSA)的相互作用,由Van’t Hoff方程计算了反应的热力学参数,并根据Stern-Volmer方程计算了不同温度下的结合位点和结合常数.结果表明,贝加因可静态猝灭BSA的内源荧光;二者相互作用的焓变和熵变均大于零,说明疏水作用力是二者之间的主要作用力.与此同时,贝加因可诱导牛血清白蛋白构象变化.相关研究结果有助于在分子水平上更好地理解药物的作用机理以及吸收和分布特性.The interaction between baicalein and bovine serum albumin（BSA） was studied by means of fluorescence spectrometry and absorption spectrometry.The thermodynamic parameters of the reaction were calculated using Van＇t Hoff equation.Besides,the number of binding sites and the apparent binding constants at different temperatures were calculated from fluorescence quenching data using Stern-Volmer equation.Results indicate that baicalein is able to quench the intrinsic fluorescence of BSA via static quenching mechanism.The changes of enthalpy and entropy for the reaction of baicalein and BSA are both above 0,which indicates that their interaction is dominated by intermolecular hydrophobic force.Moreover,baicalein is able to induce the conformational change of BSA.Relevant results could help to better understand the action mechanism as well as absorption and distribution features of drugs at molecular level.

关 键 词：贝加因 牛血清白蛋白 相互作用 分子光谱 

分 类 号：O627.12[理学—有机化学]