2 results match your criteria: "University of Warwick CV4 7AL UK m.i.gibson@warwick.ac.uk.[Affiliation]"

Article Synopsis
  • - Glycan-lectin interactions are critical in biological processes like pathogen attachment and immune response, but current methods to study these interactions are often expensive and not widely accessible.
  • - Recently developed glycosylated plasmonic nanoparticles offer a cost-effective biosensor alternative that detects glycan-protein binding through noticeable color changes, which can be analyzed with simple equipment.
  • - This research suggests optimal parameters (gold core size and polymer tether length) for using these nanoparticles, allowing lab users to efficiently investigate new glycan/protein interactions with minimal optimization needed.
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Galectins are potential biomarkers and therapeutic targets. However, galectins display broad affinity towards β-galactosides meaning glycan-based (nano)biosensors lack the required selectivity and affinity. Using a polymer-stabilized nanoparticle biosensing platform, we herein demonstrate that the specificity of immobilised lacto--biose towards galectins can be 'turned on/off' by using site-specific glycan fluorination and in some cases reversal of specificity can be achieved.

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