摘要
目的采用荧光光谱法和紫外吸收光谱法研究曲克芦丁与牛血清白蛋白(BSA)结合反应的特征。方法将曲克芦丁对BSA内源性荧光的猝灭数据分别应用Stern-Volmer方程和Lineweaver-Burk双倒数方程计算反应的荧光猝灭常数和结合常数,应用双对数方程计算结合位点数,热力学公式计算二者结合主要作用力类型,在此基础上应用Frster非辐射能量转移理论,计算曲克芦丁与BSA相互结合时给体-受体间的距离和能量转移效率。结果结果表明曲克芦丁能够有效降低BSA的内源性荧光,其猝灭机制属于静态猝灭,二者之间的结合力为疏水作用力,二者的结合常数为106数量级,结合位点数为1,作用距离为1.97nm,能量转移效率为0.529。结论曲克芦丁可与BSA通过疏水作用结合为复合物,经静态猝灭机制引起BSA内源性荧光的猝灭。
Aim To study the characteristics of the binding reaction of Troxetutin with bovine serum albumin （BSA） by fluorescence and ultra violet-visible absorption spectra.Methods The quenching mechanism of the fluorescence of BSA by troxerutin was studied with fluorescence.To determine the dynamic quenching constants and static binding constants,the Stern-Volmer equation and the double reciprocal Lineweaver-Burk equation were applied.The number of binding site was calculated with double logarithmic equation and the main binding force was discussed by thermodynamic equations.The binding distance and energy transfer efficiency between donor （BSA） and acceptor （troxerutin） were obtained based on Frster＇s nonradiative energy transfer theory.Results Troxerutin effectively quenched fluorescence of BSA via static quenching processes.The binding constant Ka was calculated to be in the order of 106,indicating a strong interaction between Troxerutin and BSA.The number of binding site was approximately equal to 1,the binding distance was 1.97 nm,the energy transfer efficiency was 0.529,and the binding force was mainly hydrophobic force.Conclusion Troxerutin effectively quenchs the intrinsic fluorescence of BSA via static quenching mechanism,and the binding is mainly driven by the hydrophobic interaction.
出处
《中国药理学通报》
CAS
CSCD
北大核心
2009年第12期1584-1588,共5页
Chinese Pharmacological Bulletin
基金
国家自然科学基金资助项目(No30472057)
北京市自然科学基金资助项目(No7052007)
北京市属高等学校人才强教计划资助项目(NoPHR201007111)
北京市科技新星计划资助项目(No2008A77)
关键词
曲克芦丁
牛血清白蛋白
荧光光谱法
相互作用
Troxerutin
bovine serum albumin
fluorescence spectrometry
interaction
