摘要
利用多种光谱技术研究了在pH7.40的Tris-HCl缓冲体系下,荷花碱与牛血清白蛋白(BSA)的相互作用。研究发现荷花碱对牛血清白蛋白有较强的荧光猝灭作用且为静态猝灭。用Stern-Volmer和Line weaver-Burk方程处理荧光猝灭数据,得到反应的结合常数在293K时为1.70×104L/mol,结合的ΔH°=-20.2kJ/mol,ΔS°=12.0J/(K.mol)。该药物与血清白蛋白之间的作用力为疏水作用和静电作用。根据Frster非辐射能量转移理论求得荷花碱与BSA相互结合时,其供体-受体间的距离为2.59nm。用圆二色谱等手段表明结合对蛋白的构象产生了影响。同时考察了中药活性成分甘草次酸和脂肪酸对结合的影响。
The interaction between neferine （NF） and bovine serum albumin （BSA） was studied under a pH 7.40 Tris-HC1 buffer system by multiple spectroscopic techniques. It is shown that NF has a powerful ability to quench the albumin＇s fluorescence in a static mode. The fluorescence quenching data were analyzed according to Stern-Volmer equation and Line weaver-Burk equation. The binding constant obtained was 1.70 × 10^4L/mol at 293 K and ΔH° = -20.2 kJ/mol, ΔH° = 12.0 J/（K ·mol）. The main sorts of binding force of NF-BSA were hydrophobic interaction and electrostatic action. The distance between donor and acceptor in BSA-NF was 2.59 nm based on the Forster energy transfer theory. Results of technique of circular dichroism etc show the binding can cause conformation change of BSA. In the mean time, effects of bioactive components from traditional Chinese medicine （glycyrrhetinic acid） and fatty acids on the binding were evaluated.
出处
《分析化学》
SCIE
CAS
CSCD
北大核心
2008年第8期1066-1070,共5页
Chinese Journal of Analytical Chemistry
基金
国家自然科学基金重点(No.20235020)
广西教育厅科研基金(No.200507217)资助项目
关键词
荷花碱
牛血清白蛋白
光谱学方法
甘草次酸
Neferine, bovine serum albumin, spectroscopic method, glycyrrhetinic acid
