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Author Spotlight: Advancing Protein Glycosylation Research Using a Fully Automated System
Published on: June 28, 2024
Self-Assembled Multi- and Single-Chain Glyconanoparticles and Their Lectin Recognition
Yamin Abdouni1, Gijs M Ter Huurne2, Gokhan Yilmaz3,4
1School of Engineering and Materials Science, Queen Mary University of London, London E1 4NS, U.K.
Abstract:
In this work, we describe the physicochemical characterization of amphiphilic glycopolymers synthesized via copper(0)-mediated reversible-deactivation radical polymerization (Cu-RDRP). Depending on the chemical composition of the polymer, these glycopolymers are able to form multi-chain or single-chain polymeric nanoparticles. The folding of these polymers is first of all driven by the amphiphilicity of the glycopolymers and furthermore by the supramolecular formation of helical supramolecular stacks of benzene-1,3,5-tricarboxamides (BTAs) stabilized by threefold hydrogen bonding. The obtained polymeric nanoparticles were subsequently evaluated for their lectin-binding affinity toward a series of mannose- and galactose-binding lectins via surface plasmon resonance. We found that addition of 2-ethylhexyl acrylate to the polymer composition results in compact particles, which translates to a reduction in binding affinity, whereas with the addition of BTAs, the relation between the nature of the particle and the binding ability system becomes more unpredictable.
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