摘要
用光谱手段研究了在pH=7.4的生理酸度条件下农药氟氰戊菊酯(FC)与牛血清白蛋白(bovine serumalbumin,BSA)之间的相互作用.荧光研究表明,FC浓度的增加会引起BSA342 nm处荧光有规律地猝灭.采用Stern-Vol mer方程分析了猝灭的机理为静态猝灭.计算了热力学参数,由焓变(ΔH<0)和熵变(ΔS<0)值推断FC与BSA之间主要靠氢键和范德华力结合.生成自由能变ΔG<0,表明此作用过程是一个自发过程.通过同步荧光和圆二色谱实验证实了结合过程中BSA构象的变化.圆二色谱实验的结果显示了BSA中的α-螺旋结构的损失,说明其微环境及构象均发生了变化.
The interaction of flucythrinate （FC） and bovine serum albumin （BSA） under physiological condition was investigated by spectroscopic methods and the quenching constants at different temperatures were measured. The fluorescence results revealed that FC caused the fluorescence quenching of BSA through a static quenching procedure at low concentrations. Thermodynamic parameters △G, △H and △S at different temperatures were calculated. The data indicated that the van der Waals force was the dominant intermolecular force in stabilizing the complex and the binding process was spontaneous. In addition,the impact of FC on the conformation of BSA was analyzed using synchronous fluorescence and circular dichroism spectroscopy. The CD spectra results showed that the α-helix content of BSA decreased. It＇s concluded that the microenvironment and conformation of BSA were changed in the binding reaction.
出处
《华中师范大学学报（自然科学版）》
CAS
CSCD
北大核心
2010年第2期243-246,250,共5页
Journal of Central China Normal University：Natural Sciences
基金
国家自然科学基金资助项目(30971948)
关键词
FC
牛血清白蛋白
荧光猝灭
团二色谱
热力学参数
flucythrinate
bovine serum albumin
fluorescence quenching
circular dichroism spectroscopy
thermodynamic parameters
