Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases
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...
| Main Authors: | , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2010
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| _version_ | 1797067778918711296 |
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| author | Fernandez-Gonzalez, M Boutureira, O Bernardes, G Chalker, J Young, M Errey, J Davis, B |
| author_facet | Fernandez-Gonzalez, M Boutureira, O Bernardes, G Chalker, J Young, M Errey, J Davis, B |
| author_sort | Fernandez-Gonzalez, M |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T22:01:13Z |
| format | Journal article |
| id | oxford-uuid:4ea6e548-f97c-47fc-af97-54bb989bab41 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:01:13Z |
| publishDate | 2010 |
| record_format | dspace |
| spelling | oxford-uuid:4ea6e548-f97c-47fc-af97-54bb989bab412022-03-26T16:02:24ZSite-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidasesJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:4ea6e548-f97c-47fc-af97-54bb989bab41EnglishSymplectic Elements at Oxford2010Fernandez-Gonzalez, MBoutureira, OBernardes, GChalker, JYoung, MErrey, JDavis, BCombined 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. |
| spellingShingle | Fernandez-Gonzalez, M Boutureira, O Bernardes, G Chalker, J Young, M Errey, J Davis, B Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases |
| title | Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases |
| title_full | Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases |
| title_fullStr | Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases |
| title_full_unstemmed | Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases |
| title_short | Site-selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases |
| title_sort | site selective chemoenzymatic construction of synthetic glycoproteins using endoglycosidases |
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