罗丹明B与牛血清白蛋白的相互作用研究  

Study on the interaction of Rhodamine B and Bovine Serum Albumin

作　　者：周享春[1] 颜承农[1] 王特[1] 宁方秀[1] 

机构地区：[1]长江大学化学与环境工程学院,湖北荆州434023

出　　处：《化学研究与应用》2009年第1期36-41,共6页Chemical Research and Application

基　　金：湖北省自然科学基金(2005ABA067;2004ABA104)资助

摘　　要：在模拟动物体生理条件和不同温度下,用荧光光谱和紫外-可见吸收光谱法研究了罗丹明B(RHB)与牛血清白蛋白(BSA)结合反应的光谱行为。试验发现,RHB对BSA有较强的荧光猝灭作用。用Stern-Volm er和L ineweaver-Burk方程分别处理试验数据,发现BSA与RHB发生反应生成了新的复合物,属于静态荧光猝灭。求出了反应时复合物的形成常数KLB(6.080×104L.mol-1)、热力学参数(ΔHθ=-5.997 kJ.mol-1,ΔSθ=72.01 J.K-1,ΔGθ=-28.09 kJ.mol-1)和结合位点数(1.025)等,证明二者主要靠静电作用力结合。同时用同步荧光光谱及三维荧光光谱法探讨了RHB对BSA构象的影响,表明RHB使色氨酸残基所处微环境的极性减弱、疏水作用增强。为阐明RHB的染色机理、毒理效应和生物学效应提供了重要信息。Under the simulated physiological condition of animal body and different temperatures, the binding of rbodamine B （RHB） to bovine serum albumin （BSA）was studied by fluorescence spectrum and ultra-violet spectrum. It was shown that this compound has a quite strong ability to quench the fluorescence launching from BSA.. After analyzing the fluorescence quenching data according to Stem-Volmer equation and Lineweaver-Burk double-reciprocal equation, we found that BSA had reacted with RHB and formed a certain new compound, the quenching belonged tO static fluorescence quenching. KLB （6. 080 × 10^4L.mol^-1）the forming constants of the compound,the thermodynamic parameters（ △H^θ= -5. 997kJ.mol^-1, △H^θ =72.01 J.K^-1, △H^θ= -28.09 kJ.mol^-1）and the number of binding sites （ 1. 025 ）were obtained,The latter shows that the binding power between them is mainly the electrostatic interactions. The effect of RHB on the con-formation of BSA was analyzed by synchronous fluorescence spectra and three-dimensional fluorescence spectra. It shows that the polarity microenvironment around Trp residues decreased, hydrophobic forces increased. Some important information was offered for enucleating the dyeing mechanisms, the toxicity effects and biological effects of RHB.

关 键 词：罗丹明B 牛血清白蛋白 荧光猝灭光谱 三维荧光光谱 热力学参数 染色机理 

分 类 号：O641.3[理学—物理化学]