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<p>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.</p>

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Versatile Glycan Probes for Multiplatform Investigation of Glycan Interactions with Proteins, Viruses, and Cells

  • 期刊论文

  • 出版模式：

    开放获取

  • 发表日期：

    2026年7月17日

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  • Jin Yu,
  • Alexiane Decout,
  • Jiayun Yang,
  • Antonio Di Maio,
  • Wengang Chai,
  • W. Bruce Turnbull,
  • Thilo Stehle,
  • Steven H. Sacks,
  • Thomas P. Peacock,
  • Munir Iqbal,
  • Ten Feizi,
  • Yan Liu

摘要

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.