Cation-pi bonding and amino-aromatic interactions in the biomolecular recognition of substituted ammonium ligands.

TitleCation-pi bonding and amino-aromatic interactions in the biomolecular recognition of substituted ammonium ligands.
Publication TypeJournal Article
Year of Publication1996
AuthorsScrutton, NS, Raine, AR
JournalBiochem J
Volume319 ( Pt 1)
Pagination1-8
Date Published1996 Oct 01
ISSN0264-6021
KeywordsAmino Acids, Animals, Cations, Drug Design, Humans, Ligands, Protein Binding, Quaternary Ammonium Compounds
Abstract

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.

DOI10.1042/bj3190001
Alternate JournalBiochem. J.
Citation Key10.1042/bj3190001
PubMed ID8870640
PubMed Central IDPMC1217726