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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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Publication details

The article was received on 02 Oct 2012, accepted on 21 Nov 2012 and first published on 04 Dec 2012


Article type: Paper
DOI: 10.1039/C2OB26938D
Citation: Org. Biomol. Chem., 2013,11, 630-639
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    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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