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- W2897833298 endingPage "770" @default.
- W2897833298 startingPage "749" @default.
- W2897833298 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." @default.
- W2897833298 created "2018-10-26" @default.
- W2897833298 creator A5038694828 @default.
- W2897833298 creator A5048635691 @default.
- W2897833298 creator A5050103864 @default.
- W2897833298 date "2018-10-11" @default.
- W2897833298 modified "2023-10-03" @default.
- W2897833298 title "Recent structural advances in constrained helical peptides" @default.
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- W2897833298 doi "https://doi.org/10.1002/med.21540" @default.
- W2897833298 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7395366" @default.
- W2897833298 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30307621" @default.
- W2897833298 hasPublicationYear "2018" @default.