摘要
利用荧光光谱法和紫外-可见光谱法研究了山姜素与人血清白蛋白(HSA)之间的相互作用。证实了山姜素对HSA的荧光猝灭为动态猝灭过程,并测定了不同温度下的猝灭常数;根据Frster非辐射能量转移理论,计算出山姜素在蛋白质中的结合位置与色氨酸残基间的距离为4.05nm;由求得的热力学参数,推断了山姜素与HSA之间主要靠疏水作用力结合;用三维荧光光谱及同步荧光光谱技术探讨了山姜素对HSA构象的影响。
The interaction between alpinetin and human serum albumin （HSA） was studied by fluorescence and UV/Vis absorption spectroscopy. The results revealed that alpinetin caused the fluorescence quenching of HSA through a dynamic quenching procedure. The quenching constant was obtained at various temperatures. The binding locality was found to be an area 4. 05 nm away from tryptophan residue in HSA based on Forster＇s non-radiation energy transfer mechanism. The binding power between alpinetin and HSA is mainly the hydrophobic interaction according to the thermodynamic parameters. The effect of alpinetin on the conformation of HSA was analyzed by three-dimensional fluorescence spectra, contour spectra and synchronous spectra.
出处
《光谱学与光谱分析》
SCIE
EI
CAS
CSCD
北大核心
2008年第4期908-912,共5页
Spectroscopy and Spectral Analysis
基金
江西省自然科学基金项目(2007GZH1924)
江西省教育厅科技计划项目(GJJ08025)
教育部长江学者和创新团队发展计划项目(IRT0540)资助
关键词
山姜素
人血清白蛋白
三维荧光光谱
热力学参数
Alpinetin
Human serum albumin
Three-dimensional fluorescence spectra
Thermodynamic parameter
