X‐ray Crystallographic and Fluorometric Analysis of the Interactions of Rhein to Human Serum Albumin. (4th October 2013)

• Record Type: Journal Article
• Authors: Li, Mei; Lee, Philbert; Zhang, Yao; Ma, ZhiYuan; Yang, Feng; Zhou, ZuPing; Wu, XiaoYang; Liang, Hong
• Is Part Of: Chemical biology & drug design. Volume 83:Number 2(2014:Feb.)
• Page Start: 167
• Page End: 173
• Publication Date: 2013-10-04
• Subjects: Drugs -- Design -- Periodicals; Pharmaceutical chemistry -- Periodicals; Biochemistry -- Periodicals; 615.19005
• DOI: 10.1111/cbdd.12208
• Languages: English
• ISSNs: 1747-0277

Abstract

<abstract abstract-type="main" id="cbdd12208-abs-0001"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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.</p> </abstract>