摘要
研究了有机染料夜蓝(NB)与牛血清白蛋白(BSA)相互作用后的荧光光谱特性。结果表明:NB对BSA的荧光产生了有规律的猝灭,并且猝灭类型属于静态猝灭;得到了二者相互作用后的结合常数和结合位点数,结合位点数大约为1,说明二者为1:1结合;经计算得到了二者反应的热力学参数,通过判断得NB与BSA之间主要靠静电和疏水作用力相结合;同步荧光光谱显示了NB更接近与BSA的色氨酸残基结合;又按照Forster非辐射能量转移的理论,得到了授体(BSA)-受体(NB)的能量转移效率和结合距离,分别为0.270和2.75 nm,说明二者之间发生了非辐射能量转移。
The interaction between night blue and bovine serum albumin was studied by fluorescence spectroscopy. The experimental results showed that the intrinsic fluorescence of BSA was quenched by NB, and the quenching mechanism of the combination of NB with BSA was a static quenching procedure. The number of binding sites and the apparent binding constants at different temperatures were obtained from the analysis of the fluorescence quenching data, and the number of binding sites was 1 approximately. The analysis of thermodynamic parameters indicated that the action process between the molecules was carried out spontaneously, and the action was caused by electrostatic and hydrophobic forces. Synchronous fluorescence showed that the binding site of NB with BSA was near to be combined by tryptophan subunit. The shortest binding distance and the energy transfer efficiency between the aceeptor （BSA） and the donor （NB）, obtained by Forster＇s nonradiative energy transfer mechanism, were 0. 270 and 2.75 nm.
出处
《分析试验室》
CAS
CSCD
北大核心
2013年第4期20-24,共5页
Chinese Journal of Analysis Laboratory
基金
国家自然科学基金项目(21175086)资助
关键词
牛血清白蛋白
夜蓝
荧光光谱法
同步荧光
Bovine serum albumin
Night blue
Fluorescence spectroscopy
Synchronous fluorescence
