荧光光谱法研究1-甲基-2,6-二苯基-哌啶酮-4与BSA的相互作用

Investigation on the Interaction of 1-Methyl-2,6-diphenyl-piperidone-4 with Bovine Serum Albumin by Fluorescence Spectroscopy

用荧光光谱法和紫外吸收光谱法研究了1-甲基-2,6-二苯基-哌啶酮-4(MPP)与牛血清白蛋白(BSA)的相互作用,并计算了结合位点数(n)、结合常数(KA)和热力学参数如ΔHθ、ΔGθ、ΔSθ等。结果表明,荧光猝灭机理为动态猝灭,MPP与BSA以1∶1结合,主要作用力是疏水力。根据F rster非辐射能量转移原理计算了MPP与BSA的结合距离。

The interaction between 1-methyl-2,6-diphenyl-piperidone-4 （MPP） and bovine serum albumin （BSA） was investigated by fluorescence and UV absorption spectroscopy. The experimental results showed that the quenching mechanism of fluorescence of BSA by MPP was a dynamic quenching procedure. The binding sites number （n）, apparent binding constant （KA） and corresponding thermodynamic parameters, such as △H^θ, △G^θ,and △S^θ, were calculated. The research results indicated that MPP bound BSA with molar ratio of 1 ： 1 and the hydrophobic interaction force played major role in the reactions. The interaction distance between BSA and MPP was obtained according to Forster theory of non-radioactive energy transfer principle.