四溴双酚-A与牛血清白蛋白相互作用的光谱学及电化学研究  

Study on the Interaction of Tetrabromobisphenol A with Bovine Serum Albumin by Spectroscopy and Electrochemistry

作　　者：李淑娟[1] 元永波[1] 刘利军[1] 

机构地区：[1]宁夏大学化学化工学院,宁夏银川750021

出　　处：《分析测试学报》2010年第11期1154-1158,1164,共6页Journal of Instrumental Analysis

基　　金：宁夏自然科学基金资助项目(NZ0915)

摘　　要：采用荧光光谱、同步荧光光谱、三维光谱和循环伏安曲线法研究了溴化阻燃剂四溴双酚-A(TBBPA)与牛血清白蛋白(BSA)的相互作用。研究表明,TBBPA对BSA的内源荧光有显著的猝灭作用,根据不同温度下TBBPA对BSA的荧光猝灭作用及室温的循环伏安曲线,证实猝灭机理为静态猝灭。运用位点模型计算出结合常数KA和结合位点数n,说明TBBPA与BSA仅有1个结合位点。由ΔH0和ΔS0分别为-33.06 kJ/mol和-64.73 J/(mol.K),推断范德华力或氢键在二者结合过程中起主要作用。并通过同步荧光光谱和三维光谱研究了TBBPA对BSA构象的影响,结果表明,TBBPA分子的引入改变了BSA疏水腔内疏水微环境,从而导致BSA的构象发生变化。The interaction of brominated flame retardant tetrabromobisphenol A （TBBPA） and bovine serum albumin （BSA） was investigated mainly by means of fluorescence quenching spectrometry, synchronous fluorescence spectrometry, three-dimensional fluorescence spectrometry and cyclic volta- mmetry（CV）. The results indicated that BSA was significantly quenched in the presence of TBBPA. According to the quenching effect of TBBPA on the fluorescence intensity of BSA under different temperatures and the CVs at the room temperature, the quenching mechanism was confirmed to be a static one. The binding constants KA and the number of binding sites n were calculated at different tem- peratures, which showed that the interaction of TBBPA and BSA only had one binding site. The thermodynamic parameters, enthalpy change △H^0 and entropy change △S^0 for the reaction, were calcu- lated to be -33.06 kJ/mol and -64.73 J/（mol.K） , respectively. Based on this, van der Waals force or hydrogen bond were confirmed to be the main binding force. The synchronous fluorescence spectra and three-dimensional fluorescence spectra of TBBPA - BSA also indicated that the addition of TBBPA would change the hydrophobic micro-environment of the hydrophobic cavity and result in the conformational variation of BSA.

关 键 词：四溴双酚-A 牛血清白蛋白 光谱 循环伏安曲线 

分 类 号：O561.3[理学—原子与分子物理] O629.73[理学—物理]