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作 者:邓少东[1] 帅欧[1] 林励[1] 肖凤霞[1] 卓嘉琳[1]
机构地区:[1]广州中医药大学中药学院,广东广州510006
出 处:《中国药理学通报》2012年第11期1620-1623,共4页Chinese Pharmacological Bulletin
基 金:国家科技支撑计划项目(No 2011BAI01B02)
摘 要:目的研究野漆树苷与人血清蛋白(HSA)的结合作用及机制。方法通过光谱法研究野漆树苷与HSA的作用机制。以能量传递原理及Lineweaver-Burk双倒数方程计算野漆树苷与HSA反应的结合常数和结合距离;以热力学参数判断其与HSA间的作用力类型;以同步荧光光谱考察野漆树苷对HSA构象的影响。结果野漆树苷与HSA反应的结合常数随温度的升高而降低;野漆树苷与HSA之间的结合距离为4.16 nm;野漆树苷与HSA的互相作用以氢键和范德华力结合为主;酪氨酸残基和色氨酸残基的特征荧光光谱峰随野漆树苷浓度的增加而产生猝灭。结论野漆树苷能与HSA结合,其荧光猝灭以静态猝灭为主。Aim To study the interaction of rhoifolin with human serum albumin(HSA) and its mechanism.Methods The binding reactions of rhoifolin with HSA were studied by spectroscopy.The binding constants and binding distances were calculated according to Lineweaver-Burk equation and Fster' energy transfer theory.Thermodynamic parameters were used to calculate the types of interaction force between HSA with rhoifolin and the technique of synchronous fluorescence spectra was used to observe the effects of rhoifolin on the conformation of HSA.Results The binding constants of rhoifolin decreased with the increasing of temperature.The binding distances of rhoifolin with HSA were 4.16 nm.Rhoifolin could interact with HSA through hydrogen bond and Vander Waals'force.Fluorescence spectra of tyrosine residue and tryptophan residue decreased with the increasing concentration of rhoifolin.Conclusions Rhoifolin can combine with HSA.It is proved that the mechanism of fluorescence quenching of HSA by rhoifolin mainly lies in static quenching.
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