阿魏酸哌嗪与牛血清白蛋白相互作用的研究

Study on interaction between piperazine ferulate and bovine serum albumin

在模拟人体生理条件下,用常规荧光光谱法和紫外-可见吸收光谱法研究阿魏酸哌嗪和牛血清白蛋白结合反应的特征,并利用同步荧光法和三维荧光法研究了阿魏酸哌嗪与牛血清白蛋白作用前后白蛋白的构象变化。研究表明:阿魏酸哌嗪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-Volmer方程求出不同温度下的结合位点数和结合常数;根据F rster非辐射能量转移理论可求出其作用距离r=2.33nm;根据基本热力学参数ΔH、ΔS和ΔG判断阿魏酸哌嗪和牛血清白蛋白主要通过氢键和范德华力发生相互作用。

The interaction between piperazine fendate and bovine serum albumin was studied at pH 7.4 by spectroscopic methods including fluorescence spectra and UV-visible absorption spectra. Synchronous fluorescence and three-dimensional fluorescence spectra were used to investigate the structure change of bovine serum albumin with the addition of piperazine femlate. It showed that the complex formation between bovine serum albumin and piperazine femlate resulted in the quenching of the intrinsic fluorescence of bovine serum albumin; The main mechanism of protein fluorescence quenching was a static quenching procedure. The binding site number n and apparent binding constant KA were measured at different temperatures according to stem-volmer equation. The distance （ r = 2.33 nm） between donor （BSA） and acceptor （PF） was obtained according to forster theory of non-radiation energy transfer. The thermodynamic parameters AH, AG and AS at different temperatures were calculated, respectively, which indicated that H- bond and Van der Waals played major roles in the interaction of PF with BSA.