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Lookup NU author(s): Felicity Frank, Dr Tom McAllisterORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2025 RSC. Protein glycosylation is one of the most abundant and complex post-translational modifications, necessitating many different approaches to fully understand the biological effects. Investigation using synthetic glycopeptides is limited by the high cost of building blocks; typically >100x more than other modified amino acids e.g. phosphorylation. We report a simple, low cost route to O-glycosylated amino acids suitable for Fmoc-SPPS in two or three steps starting from peracetylated sugars. One set of reagents can furnish either the α- or β-anomer through adjusting the equivalents and reaction time. Depending on the derivative, the cost of our route is 25-60× less than commercial alternatives and offers scope for producing modified analogues. Overall, this is a convenient and user-friendly approach to access O-glycosylated amino acids, urgently required for continued investigation of the manifold roles of glycosylation in biology.
Author(s): Frank FJ, Lawson RA, McAllister TE
Publication type: Article
Publication status: Published
Journal: RSC Chemical Biology
Year: 2025
Pages: Epub ahead of print
Online publication date: 07/05/2025
Acceptance date: 06/05/2025
Date deposited: 27/05/2025
ISSN (electronic): 2633-0679
Publisher: Royal Society of Chemistry
URL: https://doi.org/10.1039/d5cb00076a
DOI: 10.1039/d5cb00076a
Data Access Statement: The data supporting this article have been included as part of the Electronic Supplementary Information.
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