4-氨基安替吡啉席夫碱与牛血清白蛋白作用研究

Study on the Interaction between 4-Aminoantipyrine Schiff Base and Bovine Serum Albumin

以4-氨基安替吡啉与噻吩-2-甲醛为原料合成了4-氨基安替吡啉缩噻吩-2-甲醛(Q1),并通过FTIR、MS、1 H NMR对其结构进行了表征.采用荧光猝灭法和紫外-可见光谱法考察了Q1与牛血清白蛋白(BSA)的相互作用.分析了Q1与BSA的作用机理,根据热力学参数方程计算出相应的ΔH、ΔS和ΔG值,推断两者之间的作用力类型主要为氢键和范德华力;并根据Frster非辐射能量转移理论,计算出不同温度下Q1与牛血清白蛋白之间的结合距离;结合Stern-Volmer方程判断其猝灭过程主要为静态猝灭.

A novel fluorescence quencher（Q1）was synthesized by 4-aminoantipyrine and thiophene 2 formaldehyde and characterized by FT-IR.MS.1H NMR. The fluorescence quenching method and UV-visible spectrometry were employed to invest on studying the interactions between the bovine serum albumin （BSA） and the Schiff base compounds. According to thermodynamic parameters of equations, we calculated the corresponding △H、△S and AG values and inferred that the type of force BSA and Schiff base compounds were hydrogen bonds and Van der Waals force. According to the F6rster non-radiative energy transfer theory, we calculate the binding distance between the Schiff base compounds with BSA. Based on double logarithmic equation, we calculated the binding constants of the Sehiff base compounds with bovine serum albumin and the corresponding number of binding sites at different temperatures. Combining with the Stern--Volmer equation, we determined that the quenching process were static quenching.