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Issue 4, 2013
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Investigation of the ring-closing metathesis of peptides in water

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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

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Article information


Submitted
02 Oct 2012
Accepted
21 Nov 2012
First published
04 Dec 2012

Org. Biomol. Chem., 2013,11, 630-639
Article type
Paper

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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