4-硝基苯胺与人血清白蛋白相互作用的研究  

INVESTIGATION ON INTERACTION OF 4-NITROANILINE WITH HUMAN SERUM ALBUMIN

作　　者：梁彦秋[1] 邓斌[2] 刘婷婷[2] 孙鹏[2] 臧树良[2] 

机构地区：[1]沈阳化工学院环境与生物系,沈阳110142 [2]辽宁大学化学学院,沈阳110036

出　　处：《环境化学》2007年第6期845-849,共5页Environmental Chemistry

基　　金：国家自然科学基金资助项目(编号20271024)

摘　　要：通过荧光和紫外光谱法研究了4-硝基苯胺与人血清白蛋白(HSA)的作用.结果表明,4-硝基苯胺对HSA的内源荧光具有强烈的猝灭作用.猝灭机理为静态猝灭,同时伴随有非辐射能量转移的发生.根据双对数方程计算其结合常数和结合位点数.确定4-硝基苯胺与HSA有一类结合部位.根据热力学参数得出4-硝基苯胺与HSA之间的主要作用力为氢键和疏水作用力.同步荧光的结果表明,作用点位靠近色氨酸,并且使色氨酸的疏水环境增强.The interaction between 4-nitroaniline and human and absorption spectroscopy. 4-Nitroaniline can strongl serum albumin（HSA） was investigated by fluorescence y quench intrinsic fluorescence of HSA. In the mechanism discuss, it was proved that static quenching occurs together with non-radiation energy transfer. The binding constants K and the number binding site n were obtained by double-logarithm regression equation. Negative enthalpy（△H） and positive entropy（△S） values indicated that both hydrogen bond and hydrophobic forces played a major role in the binding of 4-nitroaniline and HSA. The results of synchronous fluorescence showed the polarity around tryptophan residues was decreased and the hydrophobicity was increased.

关 键 词：4-硝基苯胺 人血清白蛋白 荧光光谱 紫外光谱 

分 类 号：X132[环境科学与工程—环境科学]