龙胆苦苷与人血清白蛋白作用机制  

Study on the interaction between gentiopicroside and human serum albumin by fluorescence spectrometry

作　　者：王迎进[1] 李海平[1] 冯林雁 高燕[1] 赵雅琴[1] 

机构地区：[1]忻州师范学院化学系,山西忻州034000

出　　处：《计算机与应用化学》2014年第7期886-888,共3页Computers and Applied Chemistry

基　　金：山西省高等学校科技创新项目资助(2013149);山西省高等学校大学生创新创业训练项目(2013333)

摘　　要：在模拟生理条件下,采用荧光光谱,紫外光谱和同步荧光光谱法研究了龙胆苦苷(Gentiopicroside,GPS)与人血清白蛋白(HAS)的相互作用。结果表明:龙胆苦苷能使HSA发生内源荧光猝灭,属静态猝灭机理。在298K、303K和313K下,龙胆苦苷与HSA结合常数分别为2.161×10~5,1.402×10~5和7.502×10~4L·mol^(-1)·s^(-1),结合位点数n近似为1:热力学分析表明龙胆苦苷与HSA间结合力为氢键及范德华力;根据F(o|¨)rster非辐射能量转移理论求得二者结合距离为3.68 nm;同步荧光光谱表明龙胆苦苷主要与HSA中色氨酸残基发生相互作用,改变其周围的局部构象;金属离子的介入会影响龙胆苦苷与HSA的结合能力。The interaction of Gentiopicroside （GPS） with human serum albumin （HSA） was studied by fluorescence spectrometry, UV-Visible absorption spectrometry and synchronous fluorescence spectrometry. The results showed that GPS could induced an endogenous fluorescence quenching of HSA under a mechanism of static quenching. The binding constants were determined to be 2.161 × 10^5 （298 K）, 1.402× 10^5 （303 K） and 7.502×10^4 L.mol^-1. s^-1 （303 K）, respectively. The binding site （n） was about 1. The thermodynamic parameters suggested that the interaction forces between GPS and HSA were mainly hydrogen and vander waals force. According to FOrster nonradiation energy transfer mechanism the binding distance was estimated to be 3.68 nm. The results obtained from synchronous fluorescence spectra showed that GPS mainly interacted with tryptophan in HSA. In addition, the common ions could affected the binding constant of GPS-HSA complex.

关 键 词：龙胆苦苷 人血清白蛋白 荧光猝灭 热力学参数 

分 类 号：O657.3[理学—分析化学] O629.13[理学—化学]