摘要
应用荧光及紫外光谱法研究了次甲基蓝(MB)与牛血清白蛋白(BSA)相互作用的光谱特性。测定了19℃、29℃、39℃三个温度下的结合常数KA和结合位点数n。结果表明:MB对BSA内源荧光的猝灭机理主要为静态猝灭;以疏水作用与BSA相互作用;同步荧光技术研究了MB对BSA构象的影响,表明BSA的荧光主要源于色氨酸残基,MB对BSA的构象有影响;利用Frster偶极-偶极非辐射能量转移理论,计算了MB与BSA的作用距离及19℃、29℃、39℃三个温度下的能量转移。
The interactions between methylene blue （MB） and bovine serum albumin （BSA） were studied by fluorescence and ultraviolet-visible absorption spectra. The binding constants KA and binding sites n were measured at different temperatures. The experimental results revealed that MB had strong ability to quench the intrinsic fluorescence of BSA via a static quenching mechanism. According to themodynamic parameters,the acting forces were determined to be hydrophobic force. Based on the mechanism of the Frster energy transfer,the efficiency of energy E and transfer distance r between acceptor MB and donor BSA were obtained at different temperatures.
出处
《分析科学学报》
CAS
CSCD
北大核心
2010年第4期435-439,共5页
Journal of Analytical Science
基金
国家自然科学基金(No.20875059)
关键词
次甲基蓝
牛血清白蛋白
荧光光谱法
Methylene blue
Bovine serum albumin
Fluorescence spectra
