Interaction of isoliquiritigenin with bovine serum albumin studied by fluorescence quenching method  

荧光光谱法研究异甘草素与牛血清白蛋白之间的相互作用(英文)

作　　者：韩博[1] 龙飞[1] 于玮[1] 陈文[1] 王新春[1] 郭刚[2] 周良学[2] 

机构地区：[1]石河子大学药学院,新疆石河子832002 [2]四川大学生物治疗国家重点实验室,四川成都610041

出　　处：《Journal of Chinese Pharmaceutical Sciences》2016年第3期196-200,共5页中国药学（英文版）

基　　金：National Natural Science Foundation of China(Grant No.81560699);Scientific and Technological Project of the Science and Technology Department of Guangdong Province(Grant No.2014A020209026);Social Development Research and Technology Transfer Program(Grant No.2015AD002);Outstanding Young Scientific Personnel Training Plan of Shihezi University(Grant No.2015-ZRKXJQ08)

摘　　要：Interaction of ioliquiritigenin（ISL）, which is the main active component of a commonly used traditional Chinese medicine（TCM） Glycyrrhiza uralensis Fisch. with bovine serum albumin（BSA） has been investigated. The quenching mechanism of fluorescence of bovine serum albumin by ISL was discussed. The binding sites number n and apparent binding constant K were measured by fluorescence quenching method. The thermodynamic parameters ΔH^0, ΔG^0, ΔS^0 at different temperatures were calculated. The distance r between donor（bovine serum albumin） and acceptor（ISL） was obtained according to F？rster theory of non-radiation energy transfer. The results of synchronous fluorescence spectra and UV-vis absorption spectra show that the conformation of bovine serum albumin has been changed.异甘草素是传统中药甘草中的重要活性成分之一,本工作的目的是明确异甘草素与牛血清蛋白之间的相互作用。我们讨论了异甘草素导致牛血清蛋白荧光淬灭的机制,通过荧光淬灭法测定了结合位点数n、表观结合常数K,计算了不同温度下的热力学常数ΔH^0,ΔG^0,ΔS^0。通过F?rster理论计算了异甘草素和牛血清蛋白之间的结合距离r,同步荧光光谱和紫外可见吸收光谱表明牛血清蛋白的结构发生了改变。

关 键 词：ISOLIQUIRITIGENIN Bovine serum albumin Thermodynamic parameters Energy transfer 

分 类 号：R96[医药卫生—药理学] O657.3[医药卫生—药学]