中药成分五味子甲素及其金属离子复合物与血清白蛋白相互作用的研究  

Study on the Interactions of Chinese Medicine Component Deoxyschizandrin and Its Metal Ion Complexes with Serum Albumin

作　　者：郑茂东[1] 杨锦艳[1] 郝娟[1] 黄茜[1] 张爱平[1] 

机构地区：[1]山西医科大学药学院,山西太原030001

出　　处：《分析科学学报》2010年第4期400-404,共5页Journal of Analytical Science

基　　金：国家自然科学基金(No.20371031);山西高校科技研究开发项目(No.2007122);山西省基础研究项目(No.2010011048-1)

摘　　要：在模拟人体生理条件下,采用紫外光谱法、荧光光谱法和同步荧光光谱法研究五味子甲素及其金属离子复合物与血清白蛋白(SA)的结合作用。结果表明:五味子甲素与金属离子形成1∶1复合物;五味子甲素对SA的荧光猝灭机制为静态猝灭和非辐射能量转移;五味子甲素与牛血清白蛋白(BSA)和人血清白蛋白(HSA)的结合常数K、结合位点数n、结合距离r分别为3.58×104L·mol-1和6.42×103L·mol-1、0.944和0.993、2.18nm和1.63nm,其作用力以氢键和范德华力为主。同步荧光光谱法的结果表明:结合位点靠近色氨酸,并使色氨酸的疏水性减弱。共存金属离子对五味子甲素与SA的相互作用有一定的影响。The interactions of Chinese Medicine component deoxyschizandrin and its metal ion complexes with serum albumin have been investigated under the simulative human physiological condition by ultraviolet spectroscopy,fluorescence spectroscopy and synchronous fluorescence spectroscopy. The results of ultraviolet spectroscopy revealed that a 1：1 compound was formed between deoxyschizandrin and metal ions. The results of fluorescence spectrometry showed that the endogenous fluorescence of SA has been significantly quenched by deoxyschizandrin and the mechanism of fluorescence quenching was static quenching with non-radiation energy transfer. The binding parameters of deoxyschizandrin and SA are as follows：for BSA and HSA,the binding constants K are 3.58×104 L／5mol-1 and 6.42×103 L／5mol-1,the numbers of binding sites are 0.944 and 0.993,the binding distances r are 2.18 and 1.63 nm,respectively. And the major driving force is hydrogen bond and Vander Waals. The results of synchronous fluorescence demonstrated that the binding site was closer to tryptophan residues and the hydrophobicity of tryptophan residues was decreased. In addition,the effects of common metal ions on the interaction between deoxyschizandrin and SA has been studied.

关 键 词：五味子甲素 血清白蛋白 紫外光谱法 荧光光谱法 同步荧光光谱法 

分 类 号：O657.39[理学—分析化学]