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 |
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Pages (from-to) | 709-715 |
Number of pages | 7 |
Journal | Chemical Science |
Volume | 1 |
Issue number | 6 |
DOIs | |
Publication status | Published - 1 Dec 2010 |