荧光光谱法研究柯里拉京与人血清白蛋白之间的相互作用  

Study on Interaction of Corilagin and HSA by Fluorescence Spectroscopies

作　　者：申炳俊[1] 苗苗[2] 刘慧[2] 李萍[2] 周锦秀[2] 曹宇宁[2] 金丽虹[2] 田坚[1] SHEN Bingjun MIAO Miao LIU Hui LI Ping ZHOU Jinxiu CAO Ytming JIN Lihong TIAN Jian(Laboratory of Clean Energy Technology, Changchun University of Science and Technology, Changehun 130022 School of Life Science and Technology, Changchun University of Science and Technology, Changehun 130022)

机构地区：[1]长春理工大学清洁能源技术研究所,长春130022 [2]长春理工大学生命科学技术学院,长春130022

出　　处：《长春理工大学学报（自然科学版）》2016年第6期75-80,共6页Journal of Changchun University of Science and Technology(Natural Science Edition)

基　　金：国家自然科学基金(21153003);吉林省教育厅(201574);长春理工大学博士后基金(2014年)

摘　　要：在模拟人体血液p H条件(p H 7.4,离子强度0.1mol/L),通过荧光猝灭、位点竞争、同步荧光和三维荧光光谱等方法研究了柯里拉京(Cor)与人血清白蛋白(HSA)之间相互作用机制。结果表明:HSA的荧光能被Cor静态猝灭,两者间结合常数为2.79×103(298K)、2.22×104(304K)和8.41×104L/mol(310K)。根据Van’t Hoff方程结果显示,Cor与HSA间的作用主要为疏水作用,其作用过程为自发、吸热。基于F?rster能量转移,得知Cor与HSA间结合距离为9.33nm。位点竞争实验指出,Cor优先结合HSA的位点III。三维荧光光谱和同步荧光光谱显示,与Cor作用对HSA构象影响不显著。Under the simulative physiological conditions（p H=7.4,ionic strength 0.1mol/L） the interaction between Corilagin（Cor） and human serum albumin（HSA） was investigated by fluorescence spectroscopy,competition experiment,synchronous fluorescence and 3D fluorescence. Results showed that the main quenching mechanism between Cor and HSA was a static quenching process. All the magnitude binding constants（KA） were 2.79×103（298K）,2.22×104（304K）and 8.41×104L/mol（310K）. According to Van＇t Hoff equation,the interaction between Cor and HSA was mainly hydrophobic interaction. The binding distances between Cor and HSA was 9.33 nm based on F？rster energy transformation. It was pointed out by marker competition experiments that the primary binding site for Cor was located at site III in the HSA. 3D dimensional,synchronous and fluorescence spectrum showed that the conformation of HSA did not change apparently with the addition of Cor.

关 键 词：柯里拉京 人血清白蛋白 荧光光谱 标记竞争 

分 类 号：O657.3[理学—分析化学]