吡喃并[3,2-c]吡啶-5-酮衍生物与血清白蛋白相互作用的光谱和分子对接研究  

Study on interaction between pyrano pyridine-5-derivative and serum album by spectroscopy and molecular docking

作　　者：王鹏[1] 陈粤华[1] 冯素玲[1] 范学森[1] 张新迎[1] 

机构地区：[1]河南师范大学化学与环境科学学院,新乡453007

出　　处：《分析试验室》2012年第3期24-28,共5页Chinese Journal of Analysis Laboratory

基　　金：国家自然科学基金项目(20772025)资助

摘　　要：通过荧光光谱和紫外-可见吸收光谱法,在模拟生理条件下,研究了吡喃并[3,2-c]吡啶-5-酮衍生物-2-氨基-7-甲基-3-氰基-4-(4-甲苯)-吡喃并[3,2-c]吡啶-5-酮(AMP)与牛血清白蛋白(BSA)的相互作用。探讨了AMP对BSA的荧光猝灭过程的猝灭机理。不同温度下的Stern-Volmer曲线和紫外-可见吸收光谱表明:该衍生物主要以静态猝灭的方式使牛血清白蛋白的荧光猝灭。热力学参数表明两者之间的作用力类型主要为疏水作用力。用同步荧光技术考察了这一衍生物对牛血清白蛋白构象的影响。分子对接表明,该衍生物可能位于白蛋白的疏水腔IIA处。The interaction of pyrano [ 3,2-c ] pyridine-5-ketone derivative, 2-amino-7-methyl-3-cyano--4-（4- toluene） -pyranoid and [ 3,2-c ] pyridine-5-ketone （ AMP）, and bovine serum albumin （BSA） is studied by fluorescence and UV-vis absorption spectroscopies under physiological conditions. The mechanism of the fluorescence quenching between AMP and BSA is discussed. The results of Stern-Volmer curves at different temperatures and ultraviolet-visible absorption spectra show that the derivative mainly leads to fluorescence quenching of bovine serum albumin by static process. The thermodynamic parameters show that the main binding forces between them are hydrophobic interaction. The influence of the derivative on the conformation of bovine serum albumin was investigated by synchronization fluorescence technique. The molecular docking reveals that the possible binding site of the derivative is bound in the large hydrophobic cavity of subdomain IIA.

关 键 词：吡喃并[3 2-c]吡啶-5-酮衍生物 2-氨基-7-甲基-3-氰基-4-(4-甲苯)-吡喃并[3 2-c]吡啶-5-酮 血清白蛋白 荧光光谱 紫外-可见吸收光谱 相互作用 分子对接 

分 类 号：O657.3[理学—分析化学]