Issue 4, 2013

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 MgCl2 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.

Graphical abstract: Investigation of the ring-closing metathesis of peptides in water

Supplementary files

Article information

Article type
Paper
Submitted
02 Oct 2012
Accepted
21 Nov 2012
First published
04 Dec 2012

Org. Biomol. Chem., 2013,11, 630-639

Investigation of the ring-closing metathesis of peptides in water

S. A. Cochrane, Z. Huang and J. C. Vederas, Org. Biomol. Chem., 2013, 11, 630 DOI: 10.1039/C2OB26938D

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