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Issue 6, 2010
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Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases

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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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Supplementary files

Article information


Submitted
13 Apr 2010
Accepted
31 Aug 2010
First published
20 Oct 2010

Chem. Sci., 2010,1, 709-715
Article type
Edge Article

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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