期刊
CHEMICAL BIOLOGY & DRUG DESIGN
卷 83, 期 2, 页码 167-173出版社
WILEY
DOI: 10.1111/cbdd.12208
关键词
human serum albumin; rhein; protein-drug interaction; fluorescence spectroscopy; X-ray crystallography
资金
- Natural Science Foundation of China [31060121, 21171043]
- Natural Science Foundation of Guangxi [2012GXNSFCB053001, 2013GXNSFG-A019010]
- Guangxi 'Bagui' scholar programme
To investigate the interactions between natural drugs and human serum albumin (HSA), we performed fluorescence spectroscopy and X-ray crystallography to gain insight into binding mechanism and behaviour of rhein to HSA. Our fluorescence results demonstrated that rhein strongly binds with HSA, and other compounds may affect binding affinity of rhein to different extent. Structural analysis revealed that rhein binds to the IIA subdomain of HSA. The carboxylate group of rhein forms hydrogen bonds with Arg218 and Lys199, as well as a salt bond with Arg222. Hydroxyl group (4) of rhein forms a hydrogen bond with His242, and hydroxyl group (5) of rhein forms a hydrogen bond with Arg257. Oxygen atom (7) of rhein forms a hydrogen bond with Arg222, and oxygen atom (6) of rhein forms a hydrogen bond with H2O. Furthermore, hydroxyl group (4) of rhein also forms a hydrogen bond with H2O. Our results reveal the biochemical and structural characteristics of the interaction between rhein and HSA, providing guidance for future development of rhein-based compounds and a drug-HSA delivery system.
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