1418147-47-3Relevant academic research and scientific papers
Investigation of the ring-closing metathesis of peptides in water
Cochrane, Stephen A.,Huang, Zedu,Vederas, John C.
, p. 630 - 639 (2013)
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.
