论文部分内容阅读
利用荧光及紫外光谱法研究了生理pH条件下水溶液体系中维生素B6与牛血清白蛋白(BSA)的相互作用机制。维生素B6对牛血清白蛋白的荧光有较强的猝灭作用,其猝灭类型为静态猝灭。根据F rster的偶极-偶极非辐射能量转移理论算出供体-受体的结合距离为2.72 nm。由Linewear-Burk方程求出不同温度下反应时复合物的形成常数KLB和结合位点数n及对应温度下结合反应的热力学参数,证明二者主要靠氢键和范德华力结合。同时采用同步荧光分析技术,对蛋白质与药物结合时构象的变化进行了探讨。
The interaction between vitamin B6 and bovine serum albumin (BSA) in aqueous solution at physiological pH was studied by fluorescence and UV spectroscopy. Vitamin B6 has a strong quenching effect on the fluorescence of bovine serum albumin, and its quenching type is static quenching. The donor-acceptor binding distance was calculated to be 2.72 nm based on the Forster dipole-dipole non-radiative energy transfer theory. From the Linewear-Burk equation, the formation constants KLB and the number of binding sites n and the thermodynamic parameters of the binding reaction under different temperatures are obtained. It is proved that the two mainly depend on hydrogen bonding and van der Waals forces. At the same time, simultaneous fluorescence analysis was used to investigate the conformational changes in the combination of protein and drug.