The open-close mechanism of M2 channel protein in influenza A virus: A computational study on the hydrogen bonds and cation-pi interactions among His37 and Trp41

doi:10.1007/s11426-008-0087-3

CORC > 上海药物研究所 > 中国科学院上海药物研究所 > 药物发现与设计中心

	The open-close mechanism of M2 channel protein in influenza A virus: A computational study on the hydrogen bonds and cation-pi interactions among His37 and Trp41
	Cheng JiaGao 2; Zhu WeiLiang1,3 ; Wang Yanli 2; Yan XiuHua 1; Li Zhong 2; Tang Yun 2; Jiang HuaLiang1,2
刊名	SCIENCE IN CHINA SERIES B-CHEMISTRY
	2008-08
卷号	51 期号:8 页码:768-775
关键词	cation-pi interaction hydrogen bond noncovalent interaction ab initio calculation M2 protein
ISSN号	1006-9291
DOI	10.1007/s11426-008-0087-3
文献子类	Article
英文摘要	The M2 protein from influenza A virus is a tetrameric ion channel. It was reported that the permeation of the ion channel is correlated with the hydrogen bond network among His37 residues and the cation-pi interactions between His37 and Trp41. In the present study, the hydrogen bonding network of 4-methyl-imidazoles was built to mimic the hydrogen bonds between His37 residues, and the cation-pi interactions between 4-methyl-imidazolium and indole systems were selected to represent the interactions between His37 and Trp41. Then, quantum chemistry calculations at the MP2/6-311G** level were carried out to explore the properties of the hydrogen bonds and the cation-pi interactions. The calculation results indicate that the binding strength of the N--H center dot center dot center dot N hydrogen bond between imidazole rings is up to -6.22 kcal.mol(-1), and the binding strength of the strongest cation-pi interaction is up to -18.8 kcal.mol(-1) (T-shaped interaction) or -12.3 kcal.mol(-1) (parallel stacking interaction). Thus, the calculated binding energies indicate that it is possible to control the permeation of the M2 ion channel through the hydrogen bond network and the cation-pi interactions by altering the pH values.
WOS关键词	M(2) ION-CHANNEL ; PROTON CHANNEL ; ACTIVATION ; HISTIDINE ; SIMULATION ; COMPLEXES ; BILAYER
WOS研究方向	Chemistry
语种	英语
出版者	SCIENCE PRESS
WOS记录号	WOS:000257751300009
内容类型	期刊论文
源URL	[http://119.78.100.183/handle/2S10ELR8/272860]
专题	药物发现与设计中心
通讯作者	Zhu WeiLiang
作者单位	1.Chinese Acad Sci, Shanghai Inst Mat Med, Drug Discovery & Design Ctr, Shanghai 201203, Peoples R China; 2.E China Univ Sci & Technol, Sch Pharm, Shanghai 200237, Peoples R China; 3.E China Univ Sci & Technol, Sch Sci, Shanghai 200237, Peoples R China
推荐引用方式 GB/T 7714	Cheng JiaGao,Zhu WeiLiang,Wang Yanli,et al. The open-close mechanism of M2 channel protein in influenza A virus: A computational study on the hydrogen bonds and cation-pi interactions among His37 and Trp41[J]. SCIENCE IN CHINA SERIES B-CHEMISTRY,2008,51(8):768-775.
APA	Cheng JiaGao.,Zhu WeiLiang.,Wang Yanli.,Yan XiuHua.,Li Zhong.,...&Jiang HuaLiang.(2008).The open-close mechanism of M2 channel protein in influenza A virus: A computational study on the hydrogen bonds and cation-pi interactions among His37 and Trp41.SCIENCE IN CHINA SERIES B-CHEMISTRY,51(8),768-775.
MLA	Cheng JiaGao,et al."The open-close mechanism of M2 channel protein in influenza A virus: A computational study on the hydrogen bonds and cation-pi interactions among His37 and Trp41".SCIENCE IN CHINA SERIES B-CHEMISTRY 51.8(2008):768-775.