Glycan-Functionalized Microgels for Scavenging and Specific Binding of Lectins

Biomacromolecules. 2017 May 8;18(5):1460-1465. doi: 10.1021/acs.biomac.6b01754. Epub 2017 Apr 7.

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.

MeSH terms

  • Gels / chemical synthesis
  • Gels / chemistry*
  • Lectins / chemistry*
  • Lectins / metabolism
  • Microfluidics / methods
  • Polymerization
  • Polysaccharides / chemistry*
  • Protein Binding

Substances

  • Gels
  • Lectins
  • Polysaccharides