Related Experiment Video
Updated: Nov 1, 2025

11:21
Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
Published on: January 20, 2022
3.7K
Introducing affinity and selectivity into galectin-targeting nanoparticles with fluorinated glycan ligands
Sarah-Jane Richards1, Tessa Keenan2, Jean-Baptiste Vendeville3
1Department of Chemistry, University of Warwick CV4 7AL UK m.i.gibson@warwick.ac.uk.
Chemical Science
|June 24, 2021
Summary
Researchers developed novel fluorinated glycans on nanoparticle biosensors to improve galectin detection. This chemoenzymatic approach enhances specificity and affinity for potential diagnostic and therapeutic applications.
Area of Science:
- Biochemistry
- Materials Science
- Nanotechnology
Background:
- Galectins are crucial biomarkers and therapeutic targets.
- Current glycan-based biosensors lack specificity and affinity for galectins due to their broad binding to β-galactosides.
Purpose of the Study:
- To develop a highly selective nanoparticle biosensing platform for galectins.
- To investigate the use of site-specific glycan fluorination to modulate biosensor specificity.
Main Methods:
- A polymer-stabilized nanoparticle platform was utilized.
- Chemoenzymatic synthesis of fluorinated glycans using enzymes from *Bifidobacterium infantis* (BiGalK and BiGalHexNAcP) was performed.
- Site-specific glycan fluorination was employed to create diverse glycan structures.
Main Results:
- Demonstrated 'on/off' control of specificity for immobilized lacto-N-biose towards galectins via glycan fluorination.
- Achieved reversal of specificity in some cases.
- The chemoenzymatic approach successfully introduced structural diversity not easily attainable through chemical methods alone.
Conclusions:
- Integrating non-natural, fluorinated glycans into nanomaterials can impart unprecedented selectivity.
- This strategy holds significant potential for advancing biosensing applications, particularly for galectin detection.

