荧光光谱法研究安非他酮与人血清白蛋白的相互作用

Study on the Interaction Between Amfebutamone and Human Serum Albumin by Fluorescence Spectrum

关键词:  安非他酮  人血白蛋白  荧光猝灭  荧光光谱法

Key words:  amfebutamone  human serum albumin  fluorescence quenching  fluorescence spectrum

摘要:

目的 研究安非他酮与人血清白蛋白(human serum albumin，HSA)的相互作用。方法 通过荧光光谱法研究安非他酮对HSA的荧光猝灭光谱和同步荧光光谱的影响。由Stern-Volmer方程确定安非他酮对HSA的荧光猝灭机制，双对数方程确定反应结合位点和结合常数。根据热力学方程讨论两者间主要的作用力类型。结果 荧光猝灭光谱显示，安非他酮对HSA有猝灭作用，在17 ℃和37 ℃时的猝灭速率常数分别为5.714 8×10³和3.126 1×10³ L·mol^-1·s^-1，反应前后的焓变和熵变均<0，结合点数为1。结论 安非他酮对HSA的猝灭过程为静态猝灭，二者间的结合力主要为氢键和范德华力。

Abstract:

OBJECTIVE To explore the interaction between amfebutamone and human serum albumin(HAS). METHODS Fluorescence spectrum was used to measure the effects of amfebutamone on the fluorescence quenching spectra and synchronous fluorescence spectra of HAS. Stern-Volmer equation was used to determine the mechanism of fluorescence quenching of HAS. The binding constants were calculated according to Lineweaver-Burk equation and types of binding force were estimated by the calculation of thermodynamic parameters. RESULTS The fluorescence quenching spectra showed that amfebutamone had quenching effect on HAS. The quenching rate constants were 5.714 8×10³, 3.126 1×10³ L·mol^-1·s^-1 at 17 ℃ and 37 ℃. The enthalpy changes and entropy changs were both <0. The binding site number of amfebutamone and HSA was 1. Conclusion The fluorescence of HAS quenched by amfebutamone is static and the interaction force between them are mainly hydrogen bond and van der waals force.