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

Study on the Interaction of [Ni( Phen)( 5-Fu)_2]( NO_3)_2 and Bovine Serum Albumin by Fluorescence

作　　者：陈嘉曦[1] 李尚德[1] 吴都督[1] 安然[1] 

机构地区：[1]广东医学院药学院,广东东莞523808

出　　处：《广东微量元素科学》2014年第4期11-17,共7页Trace Elements Science

摘　　要：目的为了研究[Ni(Phen)(5-Fu)2](NO3)2配合物与牛血清白蛋白(BSA)的相互作用机理。方法以Ni(II)为中心离子,5-氟脲嘧啶(5-Fu)和邻菲啰啉(Phen)为配体,合成了[Ni(Phen)(5-Fu)2](NO3)2配合物,并利用荧光光谱考察了该配合物牛血清白蛋白(BSA)的相互作用。结果配合物与BSA作用可导致BSA内源荧光猝灭,其猝灭机理为静态猝灭,结合常数Ka=8.14×105 L·mol-1,结合位点数n=1.32,且该配合物能够猝灭BSA分子中表面91.0%的Trp残基。结论 [Ni(Phen)(5-Fu)2](NO3)2配合物是良好的BSA淬灭剂。Objective To investigate the interaction mechanism of [ Ni （ Phen ） （ 5-Fu ） 2 ] （ NO3 ） 2 with bovine serum albumin （BSA）.Methods A complex of [Ni（Phen）（5 -Fu）2]（NO3）2 was designed and synthesized using Ni （NO3）2, fluorouracil （5 -Fu）, 1, 10 -phenanthrotine （Phen） as starting materials, and it was characterized by elemental analyses and IR spectra .The interaction of [Ni（Phen） （5-Fu） 2 ] （ NO3 ） 2 with bovine serum albumin was studied using fluorescence spectroscopy in the pH 7.00 Tris -HCl buffer system .Results The research of fluorescence spectroscopy showed that these interactions resulted in the endogenous fluorescence quenching of bovine serum albumin , which belonged to a static quenching mechanism , and the complex could effect the conformation of bovine serum albumin.The quenching rate constant is 4.04 ＆#215;1 012 L＆#183; mol-1 ＆#183; s-1 , the binding constants Ka is 8.14 ＆#215;105 L＆#183; mol -1 and the binding sites of the static quenching n is 1.32.Moreover, the complex could quench 91.0% of tryptophane （ Trp ） group in the bovine serum albumin surface .Conclusions [ Ni （Phen）（5-Fu）2]（NO3）2 would be an excellent quenching reagent in the future .

关 键 词：锌(II)配合物 牛血清白蛋白 荧光光谱 

分 类 号：O657.31[理学—分析化学]