Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases

Journal article

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. © The Royal Society of Chemistry.

Authors: Fernandez-Gonzalez, M; Boutureira, O; Bernardes, G; Chalker, J; Young, M

• Publication status: Published
• Journal: CHEMICAL SCIENCE
• Volume: 1
• Issue: 6
• Pages: 709-715
• Publication date: 2010-01-01
• DOI: 10.1039/c0sc00265h
• EISSN: 2041-6539
• ISSN: 2041-6520
• Language: English