4-氨基安替吡啉缩吗啉香草醛希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

作　　者：马同森[1] 王恩泽[1] 张君丽[2] 黄齐[1] 张琳[1] 周艳梅[1] 

机构地区：[1]河南大学化学化工学院环境与分析科学研究所,河南开封475004 [2]河南大学植物逆境生物学重点实验室,河南开封475004

出　　处：《河南大学学报（自然科学版）》2015年第6期660-665,共6页Journal of Henan University:Natural Science

基　　金：国家自然科学基金项目(21576071);河南省国际科技合作项目(152102410023);河南省基础研究项目(142300410369);河南省教育厅自然科学研究项目(14A610013)

摘　　要：本文以4-氨基安替吡啉,香草醛和吗啉为原料首次合成了4-氨基安替吡啉缩吗啉香草醛(Q-2),并通过FT-IR、MS、1 H NMR对其结构进行了表征.采用紫外-可见光谱法和荧光猝灭法考察了Q-2与牛血清白蛋白(BSA)的相互作用机理.基于热力学方程计算出相应的ΔH、ΔG和ΔS值,推断出氢键和范德华力为两者之间作用力的主要类型;并基于Frster非辐射能量转移理论,计算出Q-2与牛血清白蛋白在不同温度下的结合距离;根据Stern-Volmer方程判断其猝灭过程主要为静态猝灭.In this paper,a new fluorescent quencher has been synthesized and characterized by FT-IR、MS、1 H NMR.The UV-visible spectrometry and the fluorescence intensity were applied to study the interactions between the fluorescent quencher Q-2and bovine serum albumin（BSA）.According to thermodynamic parameters of equations,the correspondingΔH,ΔS and ΔG values have been calculated,and the results showed that the type of force between the bovine serum albumin（BSA）and Schiff base compound were vander Waals force and hydrogen bonds.Based on the Frster,non-radiative energy transfer theory,the binding distance between the Schiff base compounds with bovine serum albumin has been calculated.According to double logarithmic equation,we calculated the binding constants of the Schiff base compound with bovine serum albumin and the corresponding number of binding sites at different temperatures.Combined with the Stern-Volmer equation,the quenching process was determined which was static quenching.

关 键 词：4-氨基安替吡啉 牛血清白蛋白 荧光猝灭 香草醛 

分 类 号：O656.2[理学—分析化学]