Glycan-Functionalized Microgels for Scavenging and Specific Binding of Lectins
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Updated: Mar 6, 2026

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Published on: June 28, 2024
Alexander Jans1, Ruben R Rosencrantz2, Ana D Mandić3
1DWI - Leibniz Institute for Interactive Materials, RWTH Aachen University , Forckenbeckstraße 50, 52076 Aachen, Germany.
Abstract:
Lectins are proteins with a well-defined carbohydrate recognition domain. Many microbial proteins such as bacterial toxins possess lectin or lectin-like binding domains to interact with cell membranes that are decorated with glycan recognition motifs. We report a straightforward way to prepare monodisperse and biocompatible polyethylene glycol microgels, which carry glycan motifs for specific binding to lectins. The sugar-functionalized colloids exhibit a wide mesh size and a highly accessible volume. The microgels are prepared via drop-based microfluidics combined with radical polymerization. GSII and ECL are used as model lectins that bind specifically to the corresponding carbohydrates, namely, GlcNAc and LacNAc. LacNAc microgels bind ECL with a high capacity and high affinity (Kd ≈ 0.5 to 1 μM), suggesting multivalent binding of the lectin to the LacNAc-decorated flexible microgel network. Glycan-functionalized microgels present a useful tool for lectin scavenging in biomedical applications.

