Accessibility navigation


Chemical and chemoenzymatic synthesis of glycosyl-amino acids and glycopeptides related to Trypanosoma cruzi mucins

Campo, V. L., Carvalho, I., Allman, S., Davis, B. G. and Field, R. A. (2007) Chemical and chemoenzymatic synthesis of glycosyl-amino acids and glycopeptides related to Trypanosoma cruzi mucins. Organic & Biomolecular Chemistry, 5 (16). pp. 2645-2657. ISSN 1477-0520

Full text not archived in this repository.

It is advisable to refer to the publisher's version if you intend to cite from this work. See Guidance on citing.

To link to this item DOI: 10.1039/b707772f

Abstract/Summary

This study describes the synthesis of the α- and β-linked N-acetyllactosamine (Galp-β-1,4-GlcNAc; LacNAc) glycosides of threonine (LacNAc-Thr). LacNAc-α-Thr was prepared by direct chemical coupling of a 2-azido-2-deoxy-lactose disaccharide donor to a suitable partially protected threonine unit. In contrast, stepwise chemical generation of β-linked N-acetylglucosamine followed by enzymatic galactosylation to give LacNAc-β-Thr proved effective, whereas use of a 2-azido-2-deoxy-lactose donor in acetonitrile failed to give the desired β-linked disaccharyl glycoside. This study illustrates that it is possible to overcome the inherent stereoselection for 1,2-trans chemical glycosylation with a GlcNAc donor, and that the well-established preference of bovine β-1,4-galactosyltransferase for β-linked acceptor substrates can also be overcome. Using this knowledge, short glycopeptide fragments based on T. cruzi mucin sequences, Thr-Thr-[LacNAcThr]-Thr-Thr-Gly, were synthesised. All LacNAc-based compounds outlined were shown to serve as acceptor substrates for sialylation by T. cruzi trans-sialidase.

Item Type:Article
Refereed:Yes
Divisions:No Reading authors. Back catalogue items
Life Sciences > School of Chemistry, Food and Pharmacy > School of Pharmacy > Medicinal Chemistry Research Group
ID Code:89158
Publisher:Royal Society of Chemistry

University Staff: Request a correction | Centaur Editors: Update this record

Page navigation