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 | |
| Publication status | Published - 2010 |
Fingerprint Dive into the research topics of 'Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases'. Together they form a unique fingerprint.
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