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Glycan‐protein interactions are essential biological processes with many disease‐related modulations and variations. One of the key proteins involved in tumor progression and metastasis is galectin‐3 (Gal‐3). A lot of effort is put into the development of Gal‐3 inhibitors as new therapeutic agents. The avidity of glycan‐protein interactions is strongly enhanced by multivalent ligand presentation. Multivalent presentation of glycans can be accomplished by utilizing glycopolymers, which are polymers with pendent glycan groups. For the production of glycopolymers, glycomonomers are synthesized by a regioselective, microwave‐assisted approach starting from lactose. The resulting methacrylamide derivatives are polymerized by RAFT and immobilized on gold surfaces using the trithiocarbonate group of the chain transfer agent. Surface plasmon resonance spectroscopy enables the label free kinetic characterization of Gal‐3 binding to these multivalent glycopolymers. The measurements indicate oligomerization of Gal‐3 upon exposure to multivalent environments and reveal strong specific interaction with the immobilized polymers. [ABSTRACT FROM AUTHOR]

We fabricated a simple sensor system for qualitative analysis of glycan-mediated interactions. Our main aim was to establish a ronbbust system that allowes drop-tests without complex fluidics. The test system should be usable in routine analytics in the future and bear sufficient sensitivity to detect binding events in the nanomolar range. For this, we employed optical ring resonators and coated them with high avidity glycopolymers based on N-acetylglucosamine (GlcNAc). These hydrophilic polymers are also very feasible in preventing unspecific protein adsorption. Drop-on binding studies with suitable lectins showed that glycopolymers were specifically recognized by a lectin with GlcNAc-specificity and prevented unspecific protein interactions very well. The system could be elaborated in the future for detection of glycan-mediated interactions in the biomedical field and is promising in means of multiplexed analysis and usage in routine analysis. [ABSTRACT FROM AUTHOR]