Cation-π 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-π bonding and amino-aromatic interactions often enable these molecules to associate with proteins. The role of organic cation-π 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-π 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.
Cation-π bonding and amino-aromatic interactions in the biomolecular recognition of substituted ammonium ligands
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Nigel S. SCRUTTON, Andrew R.C. RAINE; Cation-π bonding and amino-aromatic interactions in the biomolecular recognition of substituted ammonium ligands. Biochem J 1 October 1996; 319 (1): 1–8. doi: https://doi.org/10.1042/bj3190001
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