4.2 Article

Affinity and Specificity of Ciprofloxacin-Bovine Serum Albumin Interactions: Spectroscopic Approach

期刊

PROTEIN JOURNAL
卷 29, 期 4, 页码 234-241

出版社

SPRINGER
DOI: 10.1007/s10930-010-9244-6

关键词

Ciprofloxacin; Bovine serum albumin; Bind parameters; High-affinity binding site; Conformation investigation

资金

  1. National Natural Science Foundation of China [20803019, 20873096, 20921062]
  2. Research Foundation of Education Bureau of Hubei Province, China [Q20082205]
  3. Hubei Normal University Foundation, China [2007F10]

向作者/读者索取更多资源

Fluorescence spectroscopy in combination with UV-Vis absorption spectroscopy were employed to investigate the binding of an antibacterial drug Ciprofloxacin (CPFX) to bovine serum albumin (BSA) under the physiological conditions. In the discussion of the quenching mechanism, it was proved that the fluorescence quenching of BSA by CPFX is a result of the formation of CPFX-BSA complex. Binding parameters were determined using the modified Stern-Volmer equation and Scatchard equation to provide a measure of the binding affinity between CPFX and BSA. The results of thermodynamic parameters Delta G, Delta H, Delta S, at different temperatures indicate that the electrostatic interactions play a major role for CPFX-BSA association. Site marker competitive experiments indicated that the binding of CPFX to BSA primarily took place in site I. Furthermore, the effect of metal ions to CPFX-BSA system was studied, and the distance r between donor (BSA) and acceptor (CPFX) was obtained according to fluorescence resonance energy transfer (FRET). The conformation of BSA upon CPFX binding was evaluated by measuring synchronous fluorescence properties of the CPFX-BSA complex.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.2
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据