Investigation of the ring-closing metathesis of peptides in water

Stephen A Cochrane, Zedu Huang, John C Vederas

Research output: Contribution to journalArticle

13 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)630-9
Number of pages10
JournalOrganic & biomolecular chemistry
Issue number4
Early online date04 Dec 2012
Publication statusPublished - 28 Jan 2013
Externally publishedYes


  • Amino Acid Sequence
  • Hydrophobic and Hydrophilic Interactions
  • Molecular Sequence Data
  • Oxytocin
  • Peptides
  • Water
  • Journal Article
  • Research Support, Non-U.S. Gov't

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