Issue 6, 2010
From the journal:

Chemical Science

Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases†

Marta Fernández-González,a   Omar Boutureira,a   Gonçalo J. L. Bernardes,a   Justin M. Chalker,a   Matthew A. Young,a   James C. Erreya  and  Benjamin G. Davis*a  

* Corresponding authors

a Department of Chemistry, University of Oxford, Chemistry Research Laboratory, 12 Mansfield Road, Oxford, United Kingdom
E-mail: Ben.Davis@chem.ox.ac.uk
Fax: +44 (0) 1865 275674
Tel: +44 (0) 1865 275652

Abstract

Combined chemical tagging followed by Endo-A catalysed elongation allows access to homogeneous, elaborated glycoproteins. A survey of different linkages and sugars demonstrated not only that unnatural linkages can be tolerated but they can provide insight into the scope of Endo-A transglycosylation activity. S-linked GlcNAc-glycoproteins are useful substrates for Endo-A extensions and display enhanced stability to hydrolysis at exposed sites. O-CH2-triazole-linked GlcNAc-glycoproteins derived from azidohomoalanine-tagged protein precursors were found to be optimal at sterically demanding sites.

Graphical abstract: Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases

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Article information

DOI
https://doi.org/10.1039/C0SC00265H
Article type
Edge Article
Submitted
13 Apr 2010
Accepted
31 Aug 2010
First published
20 Oct 2010

Chem. Sci., 2010,1, 709-715

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Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases

M. Fernández-González, O. Boutureira, G. J. L. Bernardes, J. M. Chalker, M. A. Young, J. C. Errey and B. G. Davis, Chem. Sci., 2010, 1, 709 DOI: 10.1039/C0SC00265H

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