摘要
在模拟生物体生理条件下,利用荧光光谱、同步荧光光谱、分子模拟方法研究了不同温度下大黄酚与牛血清蛋白(BSA)之间的相互作用.实验结果表明,静态猝灭是导致大黄酚对BSA荧光猝灭的主要原因.通过计算热力学参数,可知该药物与蛋白的相互作用是一个熵增加和吉布斯自由能降低的自发过程,并由此推断大黄酚与BSA之间的作用力是以疏水相互作用为主.分子模拟研究表明:大黄酚能够进入BSA的疏水空腔,它们之间的相互作用不仅存在疏水作用,而且还有氢键作用,这与热力学分析结果基本一致.
The interaction of chrysophanol with bovine serum albumin(BSA) was investigated by fluorescence spectroscopy,synchronous fluorescence spectroscopy and molecular modeling techniques at different temperatures.The experimental results suggested that static quenching was the main reason for the fluorescence quenching process.Thermodynamic studies showed that the change for Gibbs free energy of the binding was a large negative value,which indicated that the interaction of chrysophanol with BSA was driven mainly by hydrophobic force.The results of molecular modeling indicated that there was not only hydrophobic interaction on the binding of chrysophanol to BSA,but there was also hydrogen bonding.The results of molecular modeling are in good agreement with those of spectral and thermodynamic studies.
出处
《河南师范大学学报(自然科学版)》
CAS
北大核心
2013年第3期79-82,102,共5页
Journal of Henan Normal University(Natural Science Edition)
基金
国家自然科学基金(21173071)
教育部高等学校博士点基金(20114104110002)
河南省教育厅科学技术研究重点项目(13B150082)
河南师范大学青年科学基金
关键词
牛血清蛋白
大黄酚
荧光光谱
分子模拟
bovine serum albumin
chrysophanol
fluorescence spectroscopy
molecular modeling