摘要
本文首次采用荧光光谱法研究了忍冬苷与牛血清白蛋白(BSA)在模拟人体生理条件下的相互作用。结果表明忍冬苷对BSA的荧光猝灭作用属于静态猝灭,且296K下结合常数Ka为3.82×105L.mol-1,结合位点数n为1.16;热力学分析表明二者主要靠氢键和范德华力结合;位点竞争实验则显示忍冬苷主要通过Site I与BSA相结合;最后还考察了几种常见的共存离子对相互作用的影响。
The interaction between veronicastroside and bovine serum albumin were firstly studied by fluorescence spectroscopy under simulative physiological condition in this paper.The experimental data revealed that BSA fluorescence quenching initiated by veronicastroside was belong to static quenching.The binding constant Ka was 3.82×105L·mol-1 and binding site was 1.16 at 296K.Thermodynamic analysis showed that binding powers were mainly hydrogen and vander Waals force.The competitive experiments indicated that the binding of veronicastroside to BSA primarily took place in Sudlow site I.Effects of common ions on the binding constant of veronicastroside-BSA complex were also discussed in this article.
出处
《海峡药学》
2011年第7期57-60,共4页
Strait Pharmaceutical Journal
关键词
忍冬苷
牛血清白蛋白
荧光光谱法
Veronicastroside
Bovine serum albumin
Fluorescence spectroscopy
