【摘要】 利用紫外-可见吸收光谱和荧光光谱法,在Tris-HCl缓冲溶液中考查了不同温度下镝(Dy)-L-苯丙氨酸-5-氟尿嘧啶三元配合物与牛血清白蛋白(BSA)之间的相互作用。实验表明,配合物对BSA的内源荧光猝灭为静态猝灭过程,并测定该反应在不同温度下的结合常数KA,且配合物与BSA以物质的量比1∶1结合。根据计算出的热力学参数表明,配合物和BSA之间的作用力主要是静电作用。用同步荧光技术考察了配合物对BSA构象的影响,结合位点接近于酪氨酸残基。更多还原

【Abstract】 The interaction between Dy-L-phe-5-fu ternary complex and bovine serum albumin(BSA) was investigated via ultraviolet-visible absorption spectra and fluorescence in tris-HCl buffer solutions at different temperatures.The results showed that static quenching was involved in adding complex in BSA solution.The complex reacted at a molar ratio of 1∶1 and the binding constants(KA) were determined.The interaction between complex and BSA was driven mainly by electrostatic interactions according to thermodynamic parameters.Respectively,the effect of ternary complexes on the conformation of BSA was obtained using synchronous fluorescence spectroscopy.The binding site is close to the tyrosine residue.更多还原