Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases

Marta Fernandez-Gonzalez, Omar Boutureira, Goncalo Bernardes, Justin Chalker, Matthew Young, James Errey, Benjamin Davis

    Research output: Contribution to journalArticle

    41 Citations (Scopus)

    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-CH 2-triazole-linked GlcNAc-glycoproteins derived from azidohomoalanine-tagged protein precursors were found to be optimal at sterically demanding sites.

    Original languageEnglish
    Pages (from-to)709-715
    Number of pages7
    JournalChemical Science
    Volume1
    Issue number6
    DOIs
    Publication statusPublished - 2010

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  • Cite this

    Fernandez-Gonzalez, M., Boutureira, O., Bernardes, G., Chalker, J., Young, M., Errey, J., & Davis, B. (2010). Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases. Chemical Science, 1(6), 709-715. https://doi.org/10.1039/c0sc00265h