Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases

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

doi:10.1039/c0sc00265h

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 journal › Article › peer-review

49 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 language	English
Pages (from-to)	709-715
Number of pages	7
Journal	Chemical Science
Volume	1
Issue number	6
DOIs	https://doi.org/10.1039/c0sc00265h
Publication status	Published - 1 Dec 2010

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

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AU - Fernandez-Gonzalez, Marta

AU - Boutureira, Omar

AU - Bernardes, Goncalo

AU - Chalker, Justin

AU - Young, Matthew

AU - Errey, James

AU - Davis, Benjamin

PY - 2010/12/1

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N2 - 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.

AB - 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.

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Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases

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