title: A new i, i + 3 peptide stapling system for α-helix stabilization.
abstract: We have previously shown that the incorporation of an 8-atom all-hydrocarbon 'staple' at positions i and i + 3 of a synthetic peptide results in substantial stabilization of the α-helical conformation. As part of our ongoing effort to explore the scope and utility of all-hydrocarbon stapling systems, we have investigated and report herein the properties of a new i, i + 3 stapling system that employs a 6-carbon cross-link.
authors.affiliation: Departments of Chemistry and Chemical Biology, Stem Cell and Regenerative Biology, Harvard University, Cambridge, MA, 02138, USA.
authors.forename: So Youn
authors.initials: SY
authors.lastname: Shim
authors.forename: Young-Woo
authors.initials: YW
authors.lastname: Kim
authors.forename: Gregory L
authors.initials: GL
authors.lastname: Verdine
mesh_terms: D000595:Amino Acid Sequence; D002942:Circular Dichroism; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary
chemical_list: D010455:Peptides
keywords: ring-closing metathesis; stapled peptides; α-helix