首页 | 本学科首页   官方微博 | 高级检索  
     

青藤碱与牛血清白蛋白相互作用的光谱研究
引用本文:杨健,余睿,陈杏. 青藤碱与牛血清白蛋白相互作用的光谱研究[J]. 广东药学院学报, 2011, 27(6): 571-574. DOI: 10.3969/j.issn.1006-8783.2011.06.005
作者姓名:杨健  余睿  陈杏
作者单位:1. 武汉大学人民医院 药学部,湖北 武汉,430060
2. 武汉大学 药学院,湖北 武汉,430071
基金项目:湖北省自然科学基金资助
摘    要:
目的 了解在生理条件下青藤碱与牛血清白蛋白(BSA)的相互作用.方法 采用荧光光谱和圆二色性光谱等方法,研究在生理条件下青藤碱与牛血清白蛋白(BSA)的相互作用.结果 青藤碱与牛血清白蛋白二者间的结合常数(KA)为(9.77±0.01) ×105 L· mo1-1(291 K)和(2.47±0.02)×105 L...

关 键 词:青藤碱  牛血清白蛋白  荧光光谱  圆二色性光谱

Studies on the interaction between sinomenine and bovine serum albumin by spectroscopy
YANG Jian,YU Rui,CHEN Xing. Studies on the interaction between sinomenine and bovine serum albumin by spectroscopy[J]. Academic Journal of Guangdong College of Pharmacy, 2011, 27(6): 571-574. DOI: 10.3969/j.issn.1006-8783.2011.06.005
Authors:YANG Jian  YU Rui  CHEN Xing
Affiliation:1(1.Department of Pharmacy,Renmin Hospital of Wuhan University,Wuhan 430060,China;2.School of Pharmaceutical Sciences,Wuhan University,Wuhan 430071,China)
Abstract:
Objective To investigate the interaction between the physiological protein BSA and sinomenine.Methods The interaction between sinomenine and bovine serum albumin(BSA) was investigated by fluorescence spectroscopy and Far-UV circular dichroism spectroscopy.Results The binding constants KA of sinomenine with BSA at 291 K and 301 K were(9.77±0.01)×105 L·mol-1 and(2.47±0.02)×105 L·mol-1,respectively.Based on the thermodynamic parameters,hydrogen bonding and Van Der Waals interaction play major roles in the binding process.There was only one binding site on BSA for sinomenine.The average binding distance between BSA and sinomenine was obtained(r=2.33 nm).The α-helical structure of BSA reduced from 18.4% to 15.6%,the β-sheet increased from 45.4% to 74.1%.Conclusion The results showed that sinomenine caused the fluorescence quenching of BSA through a static quenching procedure and that binding of sinomenine to BSA caused a change in its secondary structure.
Keywords:sinomenine  bovine serum albumin  fluorescence spectroscopy  far-UV circular dichroism spectroscopy
本文献已被 CNKI 维普 万方数据 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号