高等学校化学学报

高等学校化学学报

• 研究论文 • 上一篇    下一篇

利福布汀与人血清白蛋白相互作用的光谱研究

王丛霞, 叶玲, 闫芳菲, 王楠, 余沛霖   

  1. 首都医科大学化学生物学与药学院, 北京 100069
  • 收稿日期:2007-03-29 修回日期:1900-01-01 出版日期:2007-12-10 发布日期:2007-12-10
  • 通讯作者: 叶玲

Spectroscopic Studies on the Interaction Between Rifabutin and Human Serum Albumin

WANG Cong-Xia, YE Ling*, YAN Fang-Fei, WANG Nan, YU Pei-Lin   

  1. School of Chemical Biology and Pharmaceutical Sciences, Capital University of Medical Sciences, Beijing 100069, China
  • Received:2007-03-29 Revised:1900-01-01 Online:2007-12-10 Published:2007-12-10
  • Contact: YE Ling

PDF (PC)

被引次数

27

摘要： 用荧光光谱法和圆二色谱法研究了利福布汀(RB)与人血清白蛋白(HSA)的相互作用. 结果表明, RB与HSA之间的相互作用主要是疏水作用, 作用机制是静态猝灭与动态猝灭的结合. 其结合常数(Ka)在106数量级, 说明RB和HSA有很强的结合. 此外, 探讨了金属离子(Cu2+, Zn2+, Mg2+ 和Ca2+)对RB与HSA结合常数的影响. 同步荧光光谱和圆二色谱数据表明, RB可导致HSA的构象改变.

关键词: 利福布汀, 人血清白蛋白, 荧光猝灭, 圆二色谱

Abstract: The binding mechanism between Rifabutin(RB) and human serum albumin(HSA) was studied by fluorescence spectroscopy and CD. The results show that RB quenched the intrinsic fluorescence of HSA via a combination of static and dynamic quenching processes and hydrophobic interaction played a major role in stabilizing the RB-HSA complex. The binding constant Ka was calculated to be in the order of 106, indicating a strong interaction between RB and HSA. In addition, influences of metal ion(Cu2+, Zn2+, Mg2+ and Ca2+) on Ka were studied. Moreover, synchronous fluorescence spectroscopy and circular dichroism(CD)reveal the conformational change of HSA upon binding with RB.

Key words: Rifabutin(RB), Human serum albumin(HSA), Fluorescence spectroscopy, Circular dichroism

中图分类号: 

TrendMD: