Scrutton N S, Raine A R
Department of Biochemistry, University of Leicester, U.K.
Biochem J. 1996 Oct 1;319 ( Pt 1)(Pt 1):1-8. doi: 10.1042/bj3190001.
Cation-pi bonds and amino-aromatic interactions are known to be important contributors to protein architecture and stability, and their role in ligand-protein interactions has also been reported. Many biologically active amines contain substituted ammonium moieties, and cation-pi bonding and amino-aromatic interactions often enable these molecules to associate with proteins. The role of organic cation-pi bonding and amino-aromatic interactions in the recognition of small-molecule amines and peptides by proteins is an important topic for those involved in structure-based drug design, and although the number of structures determined for proteins displaying these interactions is small, general features are beginning to emerge. This review explores the role of cation-pi bonding and amino-aromatic interactions in the biological molecular recognition of amine ligands. Perspectives on the design of ammonium-ligand-binding sites are also discussed.
阳离子-π键和氨基-芳基相互作用是蛋白质结构和稳定性的重要贡献因素,并且它们在配体-蛋白质相互作用中的作用也已有报道。许多生物活性胺含有取代铵基团,阳离子-π键和氨基-芳基相互作用常常使这些分子能够与蛋白质结合。有机阳离子-π键和氨基-芳基相互作用在蛋白质识别小分子胺和肽中的作用,对于那些从事基于结构的药物设计的人员来说是一个重要课题,尽管已确定的显示这些相互作用的蛋白质结构数量不多,但一些普遍特征已开始显现。本综述探讨了阳离子-π键和氨基-芳基相互作用在胺配体生物分子识别中的作用。同时也讨论了铵配体结合位点设计的相关观点。