Yu, J., Decout, A., Yang, J. et al. (9 more authors) (2026) Versatile Glycan Probes for Multiplatform Investigation of Glycan Interactions with Proteins, Viruses, and Cells. Nature Communications. ISSN: 2041-1723 (In Press)
Abstract
Glycan-mediated interactions are vital to development, microbial colonisation, immune signalling, and cancer progression. Glycan microarrays have revolutionised glycobiology by enabling high-throughput analysis of these complex interactions, supported by techniques that reveal kinetics and dynamics in solution or at the cellular level. We introduce multifunctional glycan probes based on a tri-functional Fmoc-Amino-Azido (FAA) linker, enabling multi-platform investigation of glycan-mediated interactions. These FAA probes support glycan presentation on both covalent and non-covalent array platforms, allowing direct comparison of glycan recognition by diverse proteins. Notably, certain viral adhesins and immune lectins show a preference for the non-covalent platform. The azido group allows further functionalisation via ‘click chemistry’, enabling biotinylation for immobilisation on bio-layer interferometry biosensors for influenza virus binding, or fluorescent tagging for flow cytometry analysis of glycan-lectin interactions on cells. These versatile probes offer a unified platform for in-depth interrogation of glycan interactions using complementary approaches, with strong potential to advance glycan-based diagnostics and therapeutics.
Metadata
| Item Type: | Article |
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| Authors/Creators: |
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| 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) |
| Date Deposited: | 28 Jul 2026 11:33 |
| Last Modified: | 28 Jul 2026 11:33 |
| Status: | In Press |
| Publisher: | Nature Research |
| Identification Number: | 10.1038/s41467-026-75206-2 |
| Related URLs: | |
| Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:243870 |

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