荧光法研究牛血清白蛋白与三羟基苯基荧光酮-钼(Ⅵ)配合物探针的作用机理  

Study on the Mechanism of Interaction between TH-PF-Mo(Ⅵ) Complex and Bovine Serum Albumin by Fluorimetric Method

作　　者：黄建华[1] 马洪敏[2] 孙舒婷[2] 陈欣[2] 董海霞 魏琴[2] 

机构地区：[1]河南科技学院化工系,河南新乡453003 [2]济南大学化学化工学院,山东济南250022 [3]山东基恩医药研究有限公司,山东济南250100

出　　处：《光谱学与光谱分析》2006年第10期1899-1902,共4页Spectroscopy and Spectral Analysis

基　　金：国家自然科学基金(20577016);山东省自然科学基金(Y2004B11);山东省教育厅科技计划(03C05)资助项目

摘　　要：用荧光光谱法研究了三羟基苯基荧光酮(TH-PF)-钼(Ⅵ)配合物与牛血清白蛋白的结合反应。探讨了TH-PF-Mo(Ⅵ)配合物对蛋白质内源荧光的猝灭机理,并测定了不同温度下的结合常数,温度为25℃时,荧光猝灭法测得该反应的结合常数为K=4.78×104L.mol-1,温度为40℃时,荧光猝灭法测得该反应的结合常数为K=3.72×104L.mol-1。根据F rster非辐射能量转移理论,确定了给体-受体之间的作用距离和能量转移效率(E=0.314),并根据热力学参数确定了TH-PF-Mo(Ⅵ)配合物与牛血清白蛋白之间的作用力类型,以静电引力为主。The mechanism of interaction between bovine serum albumin （BSA） and trihydroxylphenylfluorone（TH-PF）-Mo（Ⅵ） complex in neutral solution was studied by fluorimetrie method. The mechanism of fluorescence quenching of BSA caused by （TH-PF）-Mo（Ⅵ） complex probe was investigated and the binding constants under different temperature were measured. The binding constants of the reaction at 25℃ and 40℃ were calculated by fluorimetrie method to be 4.78× 10^4 L·mol^-1 and 3.72×10^4L·mol^-1 , respectively. According to the theory of Foerster non-radiation energy transfer, the binding distance and transfer efficiency at 25℃ were calculated to he 2.89nm and 0. 314, respectively. Furthermore, the thermodynamic parameters were measured and the results indicated that electrostatic force played a major role in the interaction between TH-PF-Mo（Ⅵ） complex and BSA.

关 键 词：荧光猝灭 蛋白质 三羟基苯基荧光酮 配合物探针 作用机理 

分 类 号：O657.3[理学—分析化学]