Dolan, JP orcid.org/0000-0002-7009-2225, Machin, D, Dedola, S et al. (3 more authors) (2022) Synthesis of cholera toxin B-subunit glycoconjugates using site-specific orthogonal oxime and sortase ligation reactions. Frontiers in Chemistry. ISSN 2296-2646
Abstract
The chemoenzymatic synthesis of a series of dual N- and C-terminally functionalized cholera toxin B-subunit (CTB) glycoconjugates is described. Mucin 1 peptides bearing different levels of Tn antigen glycosylation (MUC1(Tn)) were prepared via solid-phase peptide synthesis. Using sortase-mediated ligation the MUC1(Tn) epitopes were conjugated to the C-terminus of CTB in a well-defined manner allowing for high density display of the MUC1(Tn) epitopes. This work explores the challenges of using sortase-mediated ligation in combination with glycopeptides and the practical considerations to obtain high levels of conjugation. Furthermore, we describe methods to combine two orthogonal labelling methodologies, oxime and sortase-mediated ligation, to expand the biochemical toolkit and produce dual N- and C-terminally labelled conjugates.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Keywords: | sortase, Glycopeptide, Glycoconjugates, Oxime ligation, Protein-modification, Sitespecific, transpeptidase, Neoglycoproteins, Mucin 1 (MUC1), Conjugate |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Chemistry (Leeds) > Organic Chemistry (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 23 Aug 2022 15:21 |
Last Modified: | 23 Jan 2025 10:30 |
Status: | Published online |
Publisher: | Frontiers Media |
Identification Number: | 10.3389/fchem.2022.958272 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:190168 |