摘要
在模拟人体生理条件下,利用光谱学和分子对接技术研究了秋水仙碱(Col)与醇脱氢酶(ADH)之间的相互作用机理。不同温度条件下的荧光光谱实验证明秋水仙碱能够通过氢键和范德华力与ADH结合形成复合物,从而抑制ADH的酶活力并引起ADH荧光的静态淬灭;不同温度条件下,Hill系数nH均约等于1,表明秋水仙碱对后继配体没有协同作用;同步荧光和红外光谱实验表明秋水仙碱对ADH的构象没有影响。紫外光谱和分子对接研究表明Col与乙醇类似,都是通过O上的孤对电子与ADH活性中心的Zn离子结合并进行定位。
The interactions between colchicine and alcohol dehydrogenase(ADH)were investigated by fluorescence,ultraviolet-visibleabsorption,FT-IR spectra techniques and molecular modeling method. The results indicated that the activity of ADH was inhibitedby colchicine,and the combination between them is a static quenching process. The corresponding thermodynamic parameters indicatedthat hydrogen bonds and van der Waals forces were the main binding force between colchicine and ADH. The values ofHill’s coefficients were equal to 1 approximately at different temperatures,which indicated there was almost no cooperativity in colchicinebinding with ADH. Furthermore,the primary binding for colchicine was located at Zn2+ ,in the active center of ADH wasconfirmed by ultraviolet-visible absorption spectroscopy and molecular modeling method. The effect of colchicine on the conformationof ADH was analyzed by synchronous fluorescence and FT-IR spectroscopy.
作者
庹浔
刘明浩
胡满根
杨淑玲
吕小兰
胡昱
TUO Xun;LIU Ming-hao;HU Man-gen;YANG Shu-ling;lV Xiao-lan;HU Yu*(Education Center for Basic Chemistry Experiments,College of Chemistry,Nanchang University,Nanchang 330031,China)
出处
《化学研究与应用》
CAS
CSCD
北大核心
2016年第8期1064-1069,共6页
Chemical Research and Application
基金
国家自然科学基金项目(21562031)资助
江西省科技计划项目(20133BBE50016)资助
江西省教育厅项目(GJJ10361)资助
南昌大学校基金(Z04297)资助
关键词
秋水仙碱
醇脱氢酶
相互作用
光谱法
分子对接
colchicine
alcohol dehydrogenase
interaction
spectroscopic methods
molecular modeling method