Cation-pi bonding and amino-aromatic interactions in the biomolecular recognition of substituted ammonium ligands.
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.
Scrutton
N S
NS
Department of Biochemistry, University of Leicester, U.K.
Raine
A R
AR
D000596:Amino Acids / Q000378:metabolism; D000818:Animals; D002412:Cations; D015195:Drug Design; D006801:Humans; D008024:Ligands; D011485:Protein Binding; D000644:Quaternary Ammonium Compounds / Q000737:chemistry / Q000378:metabolism*
D000596:Amino Acids; D002412:Cations; D008024:Ligands; D000644:Quaternary Ammonium Compounds