Journal
MEDICINAL RESEARCH REVIEWS
Volume 39, Issue 2, Pages 749-770Publisher
WILEY
DOI: 10.1002/med.21540
Keywords
alpha helix; helical peptides; peptide chemistry; protein-protein interactions
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Funding
- National Center for Complementary and Integrative Health [T32AT007533]
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Given the ubiquity of the ⍺-helix in the proteome, there has been much research in developing mimics of ⍺-helices, and most of this study has been toward developing protein-protein interaction inhibitors. A common strategy for mimicking ⍺-helices has been through the use of constrained, helical peptides. The addition of a constraint typically provides for conformational and proteolytic stability and, in some cases, cell permeability. Some of the most well-known strategies included are lactam formation and hydrocarbon stapling. Beyond those strategies, there have been many recent advances in developing constrained peptides. The purpose of this review is to highlight recent advances in the development of new helix-stabilizing technologies, constraint diversification strategies, tether diversification strategies, and combination strategies that create new bicyclic helical peptides.
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