Hydrogen-bonded synthetic mimics of protein secondary structure as disruptors of protein-protein interactions.
Small molecules which can mimic the key structural facets of protein secondary structure, in particular the α-helix, β-strand, and β-sheet, have been shown to be potent disruptors of protein-protein interactions. Researchers have recently taken the organizational imitation of protein secondary structure to a new level by using intramolecular hydrogen bonds as stabilizing forces in these small molecule mimetics. The inclusion of these interactions invokes a conformational bias of the system, allowing for greater control of the appearance, and thus often function, of these molecules by design.
Adler
Marc J
MJ
University of Oxford, Oxford, OX1 3TA, UK.
Jamieson
Andrew G
AG
Hamilton
Andrew D
AD
D001549:Benzamides / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D006860:Hydrogen Bonding; D018716:Molecular Mimicry; D011485:Protein Binding / Q000187:drug effects; D025941:Protein Interaction Mapping; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
D001549:Benzamides; D011506:Proteins