荧光光谱法研究芥子碱与人血清蛋白的相互作用  

Studies on Interaction between Sinapine and Human Serum Albumin by Fluorescence Spectrometry

作　　者：武嘉[1] 杨晓蕊[1] 王娜[1] 郭明[1] 

机构地区：[1]大连大学环境与化学工程学院,辽宁大连116622

出　　处：《大连大学学报》2013年第3期58-61,共4页Journal of Dalian University

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。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.

关 键 词：芥子碱 人血清白蛋白 荧光光谱法 荧光猝灭 

分 类 号：O657[理学—分析化学]