长春西汀与牛血清白蛋白相互作用研究  

Study on Interaction between Vinpocetine and Bovine Serum Albumin

作　　者：王芸 李志雄 林杰 胡晓熙 张艳军 李松良 吴俊葵[3] WANG Yun;LI Zhi-xiong;LIN Jie;HU Xiao-xi;ZHANG Yan-jun;LI Song-liang;WU Jun-kui(Guangxi Colleges and Universities Key Laboratory of Beibu Gulf Oil and natural Gas Resource Effective Utilization,College of Petroleum and Chemical Engineering,Beibu Gulf University,Guangxi Qinzhou 535011;Qinzhou Key Laboratory of Biowaste Resources for Selenium-enriched Functional Utilization,Guangxi Qinzhou 535011;The First People's Hospital of Qinzhou,Guangxi Qinzhou 535011,China)

机构地区：[1]北部湾大学石油与化工学院,广西高校北部湾石油天然气资源有效利用重点实验室,广西钦州535011 [2]钦州市生物废弃物资源富硒功能化利用重点实验室,广西钦州535011 [3]钦州市第一人民医院,广西钦州535011

出　　处：《广州化工》2019年第18期34-36,共3页GuangZhou Chemical Industry

基　　金：国家自然科学基金资助项目(51863017);大学生创新创业训练计划项目资助(201811607025,201811607016)

摘　　要：利用荧光光谱法研究了心脑血管药物长春西汀与牛血清白蛋白(BSA)的相互作用。研究结果表明长春西汀与BSA能较强地结合,生成复合物,随着长春西汀药物浓度的增加,BSA在350 nm处的内源荧光峰位及峰型基本不变,荧光强度有规律地降低,长春西汀与BSA相互作用的猝灭常数随着BSA浓度的增加而减小,其荧光猝灭类型为静态猝灭;同步荧光光谱结果表明长春西汀主要和BSA上的色氨酸残基相互作用,长春西汀能使BSA的构象发生变化。The interaction between vinpocetine and bovine serum albumin (BSA ) was studied by fluorescence spectroscopy. The results showed that vinpocetine and bovine serum albumin can combine strongly and the complex was produced. With the increasing of the concentration of vinpocetine, the peak position and the type of endogenous fluorescence of BSA were almost unchanged at 350 nm, and the fluorescence intensity decreased regularly. The quenching constant of the interaction between vinpocetine and BSA decreased with the increasing of BSA concentration. The fluorescence quenching type was static quenching. The results of synchronous fluorescence spectra showed that vinpocetine mainly interacted with tryptophan residues on BSA and vinpocetine can change the conformation of BSA.

关 键 词：长春西汀 牛血清蛋白 荧光光谱法 

分 类 号：O69[理学—化学]