[Cu(Phen)(5-Fu)_2](NO_3)_2配合物与牛血清白蛋白相互作用的荧光光谱研究  

Fluorescence spectrometric study of interaction between complex [Cu(Phen)(5-Fu)_2](NO_3)_2 and bovine serum albumin

作　　者：陈稚[1] 刘新光[1] 林晓芳[1] 谭荧飞[1] 陈伟贤[1] 冯杰雄[1] 朱敏豪[1] 吴都督[1] 

机构地区：[1]广东医学院分析中心,广东东莞523808

出　　处：《化学研究》2011年第2期25-29,共5页Chemical Research

基　　金：广东省大学生创新实验项目(KY1037);广东省卫生厅项目(B2009190)

摘　　要：以Cu(Ⅱ)作为中心离子,5-氟脲嘧啶(5-Fu)和邻菲咯啉(Phen)作为配体,合成了[Cu(Phen)(5-Fu)2](NO3)2配合物;利用元素分析和红外光谱分析了配合物的组成和化学结构;利用荧光光谱考察了其与牛血清白蛋白(BSA)的相互作用.结果表明,配合物与BSA作用可导致BSA内源荧光猝灭;其猝灭机理为静态猝灭,速率常数为7.38×1012L·mol-1·s-1,结合常数Ka=2.13×106L·mol-1,结合位点数n=1.39.与此同时,该配合物能够猝灭BSA分子表面95.4%的色氨酸(Trp)残基,是良好的BSA淬灭剂.A complex [Cu（Phen）（5-Fu）2]（NO3）2 was designed and synthesized with Cu（NO3）2,fluorouracil（5-Fu）,and 1,10-phenanthrotine（Phen） as the starting materials.The composition and chemical structure of resultant complex were analyzed by means of elemental analysis and infrared spectrometry.The interaction of [Cu（Phen）（5-Fu）2]（NO3）2 with bovine serum albumin（BSA） in Tris-HCl buffer system（pH = 6.50） was studied using fluorescence spectrometry.It was found that the interaction between the complex and BSA resulted in quenching of endogenous fluorescence of BSA.The quenching process could be described with static quenching mechanism,with quenching rate constant being 7.38×1012 L·mol-1·s-1,binding constant being 2.13×106 L·mol-1 and binding site number being 1.39.In the meantime,the complex could quench 95.4% of tryptophan（Trp） residue on the surface of BSA,showing promising potential as a candidate quenching agent for BSA.

关 键 词：铜(Ⅱ)配合物 牛血清白蛋白 相互作用 荧光光谱 

分 类 号：O623.662[理学—有机化学]