Hydrogen-bonded synthetic mimics of protein secondary structure as disruptors of protein-protein interactions.

Journal article

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.

Authors: Adler, M; Jamieson, A; Hamilton, A

• Publication status: Published
• Journal: Current topics in microbiology and immunology
• Volume: 348
• Pages: 1-23
• Publication date: 2011-01-01
• DOI: 10.1007/82_2010_91
• ISSN: 0070-217X
• Language: English
• Keywords: Protein Structure, Secondary; Benzamides; Protein Binding; Protein Interaction Mapping; Proteins; Hydrogen Bonding; Molecular Mimicry