Examination of mercaptobenzyl sulfonates as catalysts for native chemical ligation: application to the assembly of a glycosylated Glucagon-Like Peptide 1 (GLP-1) analogue

Ben Cowper; Tsz Mei Sze; Bhavesh Premdjee; Aileen F Bongat White; Andrew Hacking; Derek Macmillan

doi:10.1039/c4cc09502b

Examination of mercaptobenzyl sulfonates as catalysts for native chemical ligation: application to the assembly of a glycosylated Glucagon-Like Peptide 1 (GLP-1) analogue

Chem Commun (Camb). 2015 Feb 21;51(15):3208-10. doi: 10.1039/c4cc09502b.

Authors

Ben Cowper¹, Tsz Mei Sze, Bhavesh Premdjee, Aileen F Bongat White, Andrew Hacking, Derek Macmillan

Affiliation

¹ Department of Chemistry, University College London, 20 Gordon Street, London, WC1H 0AJ, UK. d.macmillan@ucl.ac.uk.

PMID: 25605668
DOI: 10.1039/c4cc09502b

Abstract

3/4-Mercaptobenzyl sulfonates were investigated as aryl thiol catalysts for native chemical ligation (NCL). Whilst catalysing NCL processes at a similar rate to 4-mercaptophenyl acetic acid (MPAA), the increased polarity and solubility of 3-mercaptobenzyl sulfonate in particular may favour its selection as NCL catalyst in many instances.

Publication types

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

MeSH terms

Amino Acid Sequence
Catalysis
Glucagon-Like Peptide 1 / analogs & derivatives*
Glucagon-Like Peptide 1 / chemistry*
Molecular Sequence Data
Peptides / chemistry
Sequence Analysis, Protein
Sulfhydryl Compounds / chemistry*

Substances

Peptides
Sulfhydryl Compounds
Glucagon-Like Peptide 1