Recent structural advances in constrained helical peptides. Issue 2 (11th October 2018)

• Record Type: Journal Article
• Authors: Skowron, Kornelia J.; Speltz, Thomas E.; Moore, Terry W.
• Is Part Of: Medicinal research reviews. Volume 39:Issue 2(2019)
• Page Start: 749
• Page End: 770
• Publication Date: 2018-10-11
• Subjects: alpha helix -- helical peptides -- peptide chemistry -- protein‐protein interactions; Pharmacology -- Periodicals; Drugs -- Research -- Periodicals; 615
• DOI: 10.1002/med.21540
• Languages: English
• ISSNs: 0198-6325

Abstract

Abstract: 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.