title: Promoting peptide α-helix formation with dynamic covalent oxime side-chain cross-links.
abstract: Covalent side-chain cross-linking has been shown to be a viable strategy to control peptide folding. We report here that an oxime side-chain linkage can elicit α-helical folds from peptides in aqueous solution. The bio-orthogonal bridge is formed rapidly under neutral buffered conditions, and the resulting cyclic oximes are capable of dynamic covalent exchange.
authors.affiliation: Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA.
authors.forename: Conor M
authors.initials: CM
authors.lastname: Haney
authors.forename: Matthew T
authors.initials: MT
authors.lastname: Loch
authors.forename: W Seth
authors.initials: WS
authors.lastname: Horne
mesh_terms: D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D010091:Oximes / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D014867:Water / Q000737:chemistry
chemical_list: D010091:Oximes; D010455:Peptides; D014867:Water