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荧光光谱法研究芥子碱与人血清蛋白的相互作用
引用本文:武嘉,杨晓蕊,王娜,郭明.荧光光谱法研究芥子碱与人血清蛋白的相互作用[J].大连大学学报,2013(3):58-61.
作者姓名:武嘉  杨晓蕊  王娜  郭明
作者单位:大连大学 环境与化学工程学院,辽宁 大连,116622
摘    要:在模拟生理条件下(pH=7.4),采用荧光光谱法研究了芥子碱与人血清蛋白(HSA)的相互作用。结果表明芥子碱可以使人血清蛋白的内源荧光发生猝灭。根据Stern-Volmer方程计算得到不同温度下的荧光猝灭常数,在296~303 K温度范围为静态猝灭,303~310 K为动态猝灭;由Lineweaver-Burk双倒数方程得出不同温度下芥子碱和HSA的结合常数(Ka)和结合位点数(n),并计算得到其荧光猝灭的吉布斯自由能(G)和熵值(S),其结果表明芥子碱与人血清蛋白的作用过程是一个熵增加、自由能降低的自发反应。在296~303 K时两者凭借氢键和范德华力进行结合,在303~310 K温度范围两者的主作用力为疏水作用。

关 键 词:芥子碱  人血清白蛋白  荧光光谱法  荧光猝灭

Studies on Interaction between Sinapine and Human Serum Albumin by Fluorescence Spectrometry
WU Jia , YANG Xiao-rui , WANG Na , GUO Ming.Studies on Interaction between Sinapine and Human Serum Albumin by Fluorescence Spectrometry[J].Journal of Dalian University,2013(3):58-61.
Authors:WU Jia  YANG Xiao-rui  WANG Na  GUO Ming
Institution:(College of Environment and Chemical Engineering, Dalian University, Dalian 116622, China)
Abstract:Interaction between sinapine and human serum albumin (HSA) were studied by fluorescence quenching spectroscopy at simulated physiological condition (pH=7.4). Results showed that sinapine could make a human serum albumin protein fluorescence quenching. The quench constant was calculated according to Stern-Volmer equation, indicating the process was static quench at temperature range of 296-303 K, and turned to dynamic quenching at temperature range of 303-310 K. Binding sites (n) and binding constant (Ka) were deduced between sinapine and human serum albumin through Lineweaver-Burk equation and calculated Gibbs free energy(zxG) and Entropy(aS), indicating that the reaction process between sinapine and human serum albumin was a entropy increasing, free energy decreasing spontaneous reaction. The main bonding formation of system was hydrogen and Van Der Waals force at the temperature range of 296-303 K, and after changed into hydrophobic force when the temperature stepped up to 303-310 K.
Keywords:sinapine  human serum albumin  fluorescence spectra  fluorescence quench
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