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Updated: May 29, 2026

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue
Published on: May 17, 2024
Novel Click Coupling Chemistry to Explore Glycan Recognition
Tianwei Jia1, Akul Y Mehta1, Catherine A Tilton1
1Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School, National Center for Functional Glycomics, CLS 11087-3 Blackfan Circle, Boston, Massachusetts 02115, United States.
Researchers developed a new method to attach glycans to surfaces using click chemistry. This technique enables high-throughput analysis of glycan-protein interactions and antibody responses in human serum.
Area of Science:
- Carbohydrate Chemistry
- Bioconjugation
- Immunology
Background:
- Specific recognition of glycans by proteins is crucial for biological processes and immune responses.
- Existing methods for studying glycan-protein interactions can be limited in scope and throughput.
Purpose of the Study:
- To develop a versatile and efficient method for derivatizing glycans for broad applications in biological research.
- To create platforms for high-throughput screening of glycan-binding proteins and antibody responses.
Main Methods:
- Developed a novel linker (MTZ) for bioorthogonal click chemistry-based glycan derivatization.
- Created multiplex arrays using MTZ-glycans conjugated to Luminex beads.
- Generated neoglycoproteins by coupling glycans to bovine serum albumin (BSA).
Main Results:
- Efficiently generated libraries of ABO-(H) blood group MTZ-glycans and neoglycoproteins.
- Successfully profiled antiglycan IgG, IgM, and IgA antibodies in human serum samples.
- Demonstrated the utility of neoglycoproteins in glycosyltransferase assays.
Conclusions:
- The MTZ linker and click chemistry approach provide a facile and efficient platform for exploring glycan-protein interactions.
- This technology expands the available tools for studying glycan recognition in biological and immunological contexts.
- The developed methods enable high-throughput analysis of glycan-specific antibody repertoires.
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