白杨素与人免疫球蛋白结合作用的光谱行为  

Interaction Between Chrysin and Human Immunoglobulini by Fluorescence Spectroscopy

作　　者：赵楠[1] 张国文[1] 王琳[1] 付鹏[1] 胡明明[1] 

机构地区：[1]南昌大学食品科学与技术国家重点实验室,江西南昌330047

出　　处：《南昌大学学报（理科版）》2010年第3期276-278,283,共4页Journal of Nanchang University(Natural Science)

基　　金：江西省自然科学基金资助项目(2009GZH0069);南昌大学食品科学与技术国家重点实验室基金资助项目(SKLF-TS-200917;SKLF-MB-200807);江西省科技支撑计划基金资助项目(2009BNA09000)

摘　　要：在模拟人体生理条件下,采用荧光光谱和紫外-可见吸收光谱法研究了在不同温度下,白杨素与人免疫球蛋白结合反应的光谱行为。结果表明,白杨素与人免疫球蛋白的相互作用为静态猝灭过程,求出了不同温度下的猝灭常数。根据Frster的非辐射能量转移理论,计算出白杨素在蛋白质中的结合位置与色氨酸残基间的距离为3.15nm。根据实验所得热力学参数,推断了白杨素与人免疫球蛋白之间的结合以静电作用为主,疏水作用力亦存在。同步荧光光谱显示白杨素使人免疫球蛋白构象发生了变化。Under the imitated physiological condition of human body,the interaction of chrysin with human immunoglobulini G （IgG） was studied by fluorescence and UV-vis absorption spectroscopy.The experimental results showed that only a static quenching exits between chrysin and IgG.Quenching constants and binding constants were obtained at different temperature.The binding locality was an area 3.15 nm away from tryptophan residue in IgG based on Frster＇s non-radiation energy transfer mechanism.According to the thermodynamic parameters,it showed that binding power between chrysin and IgG was mainly the electrostatic and hydrophobic interactions.The results of synchronous fluorescence spectra demonstrated that chrysin induced a conformational change of IgG.

关 键 词：白杨素 人免疫球蛋白 荧光光谱 结合反应 

分 类 号：O657.3[理学—分析化学]