C-X center dot center dot center dot H Contacts in Biomolecular Systems: How They Contribute to Protein-Ligand Binding Affinity

doi:10.1021/jp906352e

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	C-X center dot center dot center dot H Contacts in Biomolecular Systems: How They Contribute to Protein-Ligand Binding Affinity
	Lu, Yunxiang 1; Wang, Yong 1; Xu, Zhijian1 ; Yan, Xiuhua 1; Luo, Xiaoming 1; Jiang, Hualiang1 ; Zhu, Weiliang1,2
刊名	JOURNAL OF PHYSICAL CHEMISTRY B
	2009-09-17
卷号	113 期号:37 页码:12615-12621
ISSN号	1520-6106
DOI	10.1021/jp906352e
文献子类	Article
英文摘要	The hydrogen bond acceptor capability of halogens has long been underappreciated in the field of biology. In this work, we have surveyed structures of protein complexes with halogenated ligands to characterize geometrical preferences of C-X center dot center dot center dot H contacts and contributions of such interactions to protein-ligand binding C, affinity. Notably, F center dot center dot center dot H interactions in biomolecules exhibit a remarkably different behavior as compared to three other kinds of X center dot center dot center dot H (X = Cl, Br, I) interactions, which has been rationalized by means of A initio calculations using simple model systems. The C-X center dot center dot center dot H contacts in biological systems are characterized as weak hydrogen bonding interactions. Furthermore, the electrophile "head on" and nucleophile "side on" interactions of halogens have been extensively investigated through the examination of interactions in protein structures and a two-layer ONIOM-based QM/MM method. In biomolecullar systems, C-X center dot center dot center dot H contacts are recognized as secondary interaction contributions to C-X center dot center dot center dot O halogen bonds that play important roles in conferring specificity and affinity for halogenated ligands. The results presented here are within the context of their potential applications in drug design, including relevance to the development of accurate force fields for halogens.
资助项目	Hi-Tech Research and Development Program of China[2006AA02Z336] ; Postdoctoral Science Foundation of China[20080440664] ; CAS[KSCX2-YW-R-18]
WOS关键词	HALOGEN BONDING INTERACTIONS ; SIGMA-HOLE ; INTERMOLECULAR INTERACTIONS ; ACTIVE-SITE ; CATION-PI ; MOLECULAR-INTERACTIONS ; OXIDATIVE ADDITION ; CH/PI INTERACTIONS ; CRYSTAL-STRUCTURE ; HYDROGEN-BONDS
WOS研究方向	Chemistry
语种	英语
出版者	AMER CHEMICAL SOC
WOS记录号	WOS:000269655700021
内容类型	期刊论文
源URL	[http://119.78.100.183/handle/2S10ELR8/279128]
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 Sci, Shanghai 200237, Peoples R China
推荐引用方式 GB/T 7714	Lu, Yunxiang,Wang, Yong,Xu, Zhijian,et al. C-X center dot center dot center dot H Contacts in Biomolecular Systems: How They Contribute to Protein-Ligand Binding Affinity[J]. JOURNAL OF PHYSICAL CHEMISTRY B,2009,113(37):12615-12621.
APA	Lu, Yunxiang.,Wang, Yong.,Xu, Zhijian.,Yan, Xiuhua.,Luo, Xiaoming.,...&Zhu, Weiliang.(2009).C-X center dot center dot center dot H Contacts in Biomolecular Systems: How They Contribute to Protein-Ligand Binding Affinity.JOURNAL OF PHYSICAL CHEMISTRY B,113(37),12615-12621.
MLA	Lu, Yunxiang,et al."C-X center dot center dot center dot H Contacts in Biomolecular Systems: How They Contribute to Protein-Ligand Binding Affinity".JOURNAL OF PHYSICAL CHEMISTRY B 113.37(2009):12615-12621.