Incomplete functionalization of glycodendrimers: Effects on binding affinity with wheat germ agglutinin

Multivalent glycoconjugates are critical tools for elucidating lectin interactions and for designing inhibitors that target lectin-mediated biological processes. In this study, pentavalent N-acetylglucosamine (GlcNAc) carbosilane dendrimers (1a∼1c) were synthesized and efficiently isolated as intermediates during the production of hexavalent GlcNAc carbosilane dendrimers (2a∼2c) using recycling gel permeation chromatography. Although these pentavalent glycodendrimers were previously separable, they had not been thoroughly characterized. Here, their binding interactions with wheat germ agglutinin (WGA) were examined via fluorometric titration assays, revealing comparable binding affinities to those of their hexavalent counterparts. Statistical analysis further demonstrated significant differences in binding behavior between pentavalent and hexavalent glycodendrimers, as well as the effects of spacer length on lectin interactions. These findings show that partial glycosylation retains strong lectin-binding capacity and provide new insights into the interplay among valency, spacer length, and the overall architecture of glycodendrimers in glycan–lectin interactions.