Glycan-Functionalized Microgels for Scavenging and Specific Binding of Lectins

• Published in: Biomacromolecules Vol. 18; no. 5; pp. 1460 - 1465
• Main Authors: Jans, Alexander, Rosencrantz, Ruben R, Mandić, Ana D, Anwar, Naveed, Boesveld, Sarah, Trautwein, Christian, Moeller, Martin, Sellge, Gernot, Elling, Lothar, Kuehne, Alexander J. C
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 08.05.2017
• Subjects: bacterial toxins; carbohydrates; cell membranes; colloids; Gels - chemical synthesis; Gels - chemistry; lectins; Lectins - chemistry; Lectins - metabolism; microbial proteins; Microfluidics - methods; polyethylene glycol; Polymerization; Polysaccharides - chemistry; Protein Binding
• DOI: 10.1021/acs.biomac.6b01754
• ISSN: 1525-7797; 1526-4602

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 (K d ≈ 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.