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3.63×10^6L/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.