title: Investigation of the ring-closing metathesis of peptides in water.
abstract: A systematic study of the ring-closing metathesis (RCM) of unprotected oxytocin and crotalphine peptide analogues in water is reported. The replacement of cysteine with S-allyl cysteine enables RCM to proceed readily in water containing excess MgCl(2) with 30% t-BuOH as a co-solvent. The presence of the sulfur atom is vital for efficient aqueous RCM to occur, with non-sulfur containing analogues undergoing RCM in low yields.
authors.affiliation: Department of Chemistry, University of Alberta, Edmonton, Alberta, Canada T6G 2G2.
authors.forename: Stephen A
authors.initials: SA
authors.lastname: Cochrane
authors.forename: Zedu
authors.initials: Z
authors.lastname: Huang
authors.forename: John C
authors.initials: JC
authors.lastname: Vederas
mesh_terms: D000595:Amino Acid Sequence; D057927:Hydrophobic and Hydrophilic Interactions; D008969:Molecular Sequence Data; D010121:Oxytocin / Q000031:analogs & derivatives* / Q000138:chemical synthesis*; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry*; D014867:Water / Q000737:chemistry*
chemical_list: D010455:Peptides; C533006:crotalphine; D014867:Water; D010121:Oxytocin