期刊
BIOMACROMOLECULES
卷 11, 期 12, 页码 3341-3351出版社
AMER CHEMICAL SOC
DOI: 10.1021/bm100814n
关键词
-
资金
- European Union [FP6-LSH-2004-2.3.0-7, 018602]
- French ANR agency
- Fondation Pierre Fabre
The binding affinity of human scrum albumin (HSA) to three antimalarial indolone-N-oxide derivatives, INODs, was investigated under simulated physiological conditions using fluorescence spectroscopy in combination with UV-vis absorption and circular dichroism (CD) spectroscopy. Analysis of fluorescence quenching data of HSA by these compounds at different temperatures using Stern-Volmer and Lineweaver-Burk methods revealed the formation of a ground state indolone-HSA complex with binding affinities of the order 10(4) M-1. The thermodynamic parameters Delta G, Delta H, and Delta S, calculated at different temperatures, indicated that the binding reaction was endothermic and hydrophobic interactions play a major role in this association. The conformational changes of HSA were investigated qualitatively using synchronous fluorescence and quantitatively using CD. Site marker competitive experiments showed that the binding process took place primarily at site 1 (subdomain IIA) of HSA. The number of binding sites and the apparent binding constants were also studied in the presence of different ions.
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。
推荐
暂无数据