X‐ray Crystallographic and Fluorometric Analysis of the Interactions of Rhein to Human Serum Albumin
X‐ray Crystallographic and Fluorometric Analysis of the Interactions of Rhein to Human Serum Albumin
复制标题
大黄酸与人血清白蛋白相互作用的 X 射线晶体学和荧光分析
DOI：
10.1111/cbdd.12208
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发表时间：
2014
影响因子：
3
通讯作者：
Hong Liang
中科院分区：
文献类型：
--
作者：
Mei Li;Philbert Lee;Yao Zhang;Zhiyuan Ma;Feng Yang;Zuping Zhou;Xiaoyang Wu;Hong Liang
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.
DOI：
10.1073/pnas.0506440102
发表时间：
2005-12-13
影响因子：
11.1
作者：
Simard, JR;Zunszain, PA;Hamilton, JA
通讯作者：
Hamilton, JA