荧光各向异性结合同步荧光法研究1-羟基芘与牛血清白蛋白的相互作用  

Interaction of 1-Hydroxypyrene with BSA Using Fluorescence Anisotropy and Synchronous Fluorescence Analysis Methods

作　　者：张静 陈薇晓 张唯[1] 段滢[1] 朱玉秀[1] 朱亚先[3] 张勇 

机构地区：[1]近海海洋环境科学国家重点实验室,厦门大学环境与生态学院,厦门361102 [2]北京大学城市与环境学院,北京100871 [3]厦门大学化学化工学院化学系,厦门361005 [4]漳州职业技术学院,漳州363000

出　　处：《高等学校化学学报》2015年第8期1511-1516,共6页Chemical Journal of Chinese Universities

基　　金：国家自然科学基金(批准号:21075102,21177102);中央高校基本科研业务费专项资金(批准号:2013121052);国家级大学生创新创业项目基金(批准号:DC2013035)资助~~

摘　　要：在模拟生理条件下,应用荧光各向异性法研究了多环芳烃(PAHs)代谢标志物1-羟基芘(1-OHP)与牛血清白蛋白(BSA)的相互作用,并结合同步荧光法研究作用过程中BSA的构型变化,初步探讨了二者的结合方式.研究结果表明,1-OHP与BSA有较强的结合作用,形成1∶1复合物,平均结合平衡常数为3.63×106L/mol,且其结合作用强弱随着BSA浓度大小发生变化.1-OHP可与BSA的色氨酸残基结合,使BSA构型发生变化,进而使色氨酸残基周围环境的疏水性降低.Fluorescence anisotropy was employed to investigate the interaction of 1-hydroxypyrene（ 1-OHP）,the metabolism biomarker of PAHs in vivo,with a model transport protein of bovine serum albumin（ BSA）under simulated physiological conditions. Combined with synchronous fluorescence spectra,the conformation transition of BSA was also investigated. The experiment results showed that 1-OHP can bind to BSA strongly and a 1 ∶ 1 complex was formed,with an average binding equilibrium constant of 3.63×10^6L / mol. Also as the amounts of BSA differ,the interaction of 1-OHP and BSA was dominated by strong and weak binding modes alternately. Moreover,1-OHP can bind to tryptophan residues and induce the conformational and microenvironmental changes of BSA,increasing the tryptophan residue of BSA exposuring to a less hydrophobic micro-environment.

关 键 词：荧光各向异性 1-羟基芘 牛血清白蛋白 结合常数 构型变化 作用方式 

分 类 号：O657[理学—分析化学] O625[理学—化学]