Investigation of the ring-closing metathesis of peptides in water

Stephen A Cochrane; Zedu Huang; John C Vederas

doi:10.1039/c2ob26938d

Investigation of the ring-closing metathesis of peptides in water

Stephen A Cochrane, Zedu Huang, John C Vederas

Research output: Contribution to journal › Article › peer-review

19 Citations (Scopus)

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 MgCl(2) 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.

Original language	English
Pages (from-to)	630-9
Number of pages	10
Journal	Organic & biomolecular chemistry
Volume	11
Issue number	4
Early online date	04 Dec 2012
DOIs	https://doi.org/10.1039/c2ob26938d
Publication status	Published - 28 Jan 2013
Externally published	Yes

Keywords

Amino Acid Sequence
Hydrophobic and Hydrophilic Interactions
Molecular Sequence Data
Oxytocin
Peptides
Water
Journal Article
Research Support, Non-U.S. Gov't

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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 MgCl(2) 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.",

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AU - Huang, Zedu

AU - Vederas, John C

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AB - 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 MgCl(2) 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.

KW - Amino Acid Sequence

KW - Hydrophobic and Hydrophilic Interactions

KW - Molecular Sequence Data

KW - Oxytocin

KW - Peptides

KW - Water

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

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DO - 10.1039/c2ob26938d

M3 - Article

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SN - 1477-0520

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SP - 630

EP - 639

JO - Organic & biomolecular chemistry

JF - Organic & biomolecular chemistry

IS - 4

ER -

Investigation of the ring-closing metathesis of peptides in water

Abstract

Keywords

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