Gold Nanoparticle Glycointerfaces Functionalized with Alternating Glycopolymers Bearing Periodically Arranged Pendant Carbohydrate Residues

Alternating glycopolymers bearing periodically arranged pendant carbohydrate residues were synthesized by reversible addition–fragmentation chain transfer (RAFT) copolymerization of maltose-containing vinyl ether (MalVE) and ethyl maleimide (EtMI). The resulting trithiocarbonate-terminated polymers were subsequently converted into thiol-terminated glycopolymers through post-polymerization end-group transformation. These structurally well-defined alternating glycopolymers were immobilized onto gold nanoparticles (AuNPs) via Au–S interactions to construct glycopolymer-functionalized glycointerfaces. Surface functionalization of the AuNPs was confirmed by an increase in hydrodynamic diameter from approximately 42 to 59 nm after polymer immobilization. The resulting glycopolymer-functionalized AuNPs exhibited concentration-dependent lectin-mediated aggregation behavior in the presence of concanavalin A, accompanied by characteristic red shifts and broadening of the localized surface plasmon resonance (LSPR) band arising from multivalent carbohydrate–lectin interactions at the nanoparticle interface. Although the apparent association constants obtained for free alternating glycopolymers using fluorescently labeled lectin cannot be directly compared with those obtained from LSPR-based aggregation assays of AuNP-immobilized glycopolymers, the values increased from the order of 10⁵ L mol⁻¹ in solution to the order of 10⁷ L mol⁻¹ at the nanoparticle interface. This trend suggests that immobilization onto AuNPs enhances multivalent carbohydrate–lectin interactions through multivalent presentation of the glycopolymer chains at the nanoparticle interface. As a control experiment, peanut agglutinin (PNA), which does not recognize maltose residues, was added to the glycopolymer-functionalized AuNPs. No significant LSPR shift or spectral broadening was observed, indicating that nanoparticle aggregation was not induced by nonspecific lectin addition but arose from specific interactions between maltose residues and Con A. Quantitative analysis suggested that polymer chain length may influence the aggregation behavior. These results demonstrate that alternating glycopolymers provide a useful platform for constructing sequence-regulated glycointerfaces and for investigating multivalent biomolecular interactions at nanoparticle surfaces.