光谱法结合分子对接研究萘酰亚胺衍生物与牛血清白蛋白的相互作用  

Study of the interaction of naphthalimide derivative with bovine serum albumin by spectroscopy and molecular docking

作　　者：王震[1] 贾丽华[1] 杨瑞[1] 王金平[1] 郭祥峰[1,2] WANG Zhen;JIA Lihua;YANG Rui;WANG Jinping;GUO Xiangfeng(College of Chemistry&Chemical Engineering,Qiqihar University,Qiqihar 161006;Guangdong University of Petrochemical Technology,Maoming 525000)

机构地区：[1]齐齐哈尔大学化学与化学工程学院,齐齐哈尔161006 [2]广东石油化工学院,茂名525000

出　　处：《分析试验室》2020年第8期936-941,共6页Chinese Journal of Analysis Laboratory

基　　金：黑龙江省省属高校基本科研业务费科研项目(135409305,135309116)资助。

摘　　要：通过多种光谱方法并结合分子对接研究了萘酰亚胺衍生物(XYFS)与牛血清白蛋白(BSA)之间的相互作用。测试了体系在不同温度下的荧光和吸收光谱,以及时间分辨荧光光谱,发现两者之间主要通过静电作用相互结合,XYFS对BSA的荧光猝灭为静态猝灭。进一步研究了体系的同步荧光光谱和圆二色光谱,随着体系中XYFS浓度的逐渐增大,BSA构象发生了明显变化,其疏水性氨基酸残基逐渐裸露,且BSA的α-螺旋含量增加。分子对接模拟表明XYFS与BSA在SiteⅠ位结合,XYFS与BSA中的精氨酸残基有静电相互作用力。研究结果有助于深入了解萘酰亚胺衍生物与蛋白质相互作用机理及结合特征。The interaction between naphthalimide derivative(XYFS)and bovine serum albumin(BSA)was investigated by a variety of spectroscopic methods in conjunction with molecular docking.The fluorescence and absorption spectra of the system at different temperature and time-resolved fluorescence spectra were tested.It was found that the two were mainly combined by electrostatic interaction.The fluorescence quenching of BSA by XYFS was static quenching.The simultaneous fluorescence spectra and circular dichroism spectra of the system were further studied.It was found that the conformation of BSA changed significantly with the increasing of XYFS in the system,the hydrophobic amino acid residues gradually exposed and theα-helix content of BSA increased.Molecular docking simulations showed that XYFS binds to BSA at Site I,and XYFS has electrostatic interaction with arginine residues in BSA.The results of this study will help to understand the mechanism and binding characteristics of the reaction between naphthalimide derivatives and proteins.

关 键 词：光谱 牛血清白蛋白 萘酰亚胺 相互作用 

分 类 号：O657.3[理学—分析化学]