CAJ | 학술논문

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。
목적：위료연구[Ni（Phen）（5-Fu）2]（NO3）2배합물여우혈청백단백（BSA）적상호작용궤리。방법이Ni（II）위중심리자，5-불뇨밀정（5-Fu）화린비라람（Phen）위배체，합성료[Ni （Phen）（5-Fu）2]（NO3）2배합물，병이용형광광보고찰료해배합물우혈청백단백（BSA）적상호작용。결과배합물여BSA작용가도치BSA내원형광졸멸，기졸멸궤리위정태졸멸，결합상수Ka＝8.14×105 L· mol-1，결합위점수n＝1.32，차해배합물능구졸멸BSA분자중표면91.0％적Trp잔기。결론[Ni（Phen）（5-Fu）2]（NO3）2배합물시량호적BSA쉬멸제。
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 ×1 012 L· mol-1 · s-1 , the binding constants Ka is 8.14 ×105 L· 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 .