Investigation of the ring-closing metathesis of peptides in water?

Organic & Biomolecular Chemistry Pub Date: 2012-12-04 DOI: 10.1039/C2OB26938D

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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