芬布芬与牛血清白蛋白相互作用的荧光光谱检测  

Spectroscopic Studies on The Interaction Between Fenbufen and Bovine Serum Albumin

作　　者：敖登高娃[1] 金迎春[1] 

机构地区：[1]内蒙古大学化学化工学院,内蒙古呼和浩特010021

出　　处：《发光学报》2011年第4期404-410,共7页Chinese Journal of Luminescence

基　　金：国家自然科学基金(20461002);内蒙古自然科学基金(2009MS0206)资助项目

摘　　要：在模拟生理条件下,用荧光光谱法和紫外-可见吸收光谱法研究芬布芬(FBF)和牛血清白蛋白(BSA)结合反应的特征。研究表明:芬布芬与牛血清白蛋白形成复合物,从而猝灭牛血清白蛋白的内源性荧光,该过程为静态猝灭过程。根据Stern-Vlmer方程得出了不同温度下结合位点数和结合常数;根据F rster非辐射能量转移理论得出了不同温度下的作用距离;通过计算相应的热力学参数,确定了芬布芬与牛血清白蛋白之间的作用力主要为静电引力。利用同步荧光光谱及三维荧光光谱法探讨了芬布芬与牛血清白蛋白作用前后白蛋白的构型变化,以及共存金属离子对芬布芬与牛血清白蛋白结合常数的影响。The interaction between Fenbufen and bovine serum albumin（BSA） was studied with fluorescence spectra and UV-visible absorption spectra in the presence of simulating physiological systems.It showed that the complex formated by BSA and Fenbufen lead to the static quenching of the intrinsic fluorescence of BSA.The binding site number n and apparent binding constant KA were measured according to Stern-Volmer equation.The distance between BSA and Fenbufen was obtained based on the Frster nonradiative energy transfer theory.We also confirmed that the main sorts of binding force between Fenbufen and BSA is electrostatic force.Meanwhile,synchronous fluorescence and three-dimensional fluorescence spectra were used to investigate the structure change of BSA before and after the introduction of Fenbufen.Furthermore,the effect of coexistence metal ions on the binding constants of Fenbufen with BSA was also discussed.

关 键 词：芬布芬 牛血清白蛋白 相互作用 荧光光谱 紫外光谱 

分 类 号：O482.31[理学—固体物理] O657.3[理学—物理]