Canadian Journal of Chemistry · 1997 · 43 citations · 0 references
Life SciencesBiochemistryChemistryCarbohydrate ChemistryGlycobiologyStructure-activity RelationshipsCarbohydrate ReactivityCarbohydrate RecognitionGlycan BiosynthesisGlycan RecognitionGlycan StructureProtein GlycosylationAnimal LectinsBinding StudiesLectin-carbohydrate InteractionsLectinsMicrobial LectinsMultivalency EffectsSialic Acid RecognitionSynthetic Glycan Ligands
Hyperbranched glycodendrimers containing sialic acid residues were synthesized in order to further understand the multivalency effect and its role in carbohydrate–protein interactions. Gallic acid 7 as trivalent core and oligoethylene glycol derivatives as hydrophilic spacers were used to scaffold the dendritic backbones. α-Thiosialoside 16 was conjugated onto N-chloroacetylated dendritic precursors 13,14, and 26 by nucleophilic substitution to afford trivalent 17,18, and nonavalent 27 sialodendrimers. Complete sugar deprotection furnished water-soluble α-thiosialodendrimers 21,22, and 29, which were used in protein-binding studies. Turbidimetric analysis confirmed the strong potential of sialodendrimers 29 having nine readily accessible sialic acid residues to bind, cross-link, and precipitate two different lectins. Preliminary results indicated that nonavalent α-sialodendrimer 29 had a greater affinity towards dimeric wheat germ agglutinin (WGA) and the lectin from the slug Limaxflavus (LFA) than the corresponding trivalent glycodendrimers 21 and 22. Keywords: carbohydrate, dendrimer, sialic acid, gallic acid, lectin, wheat germ agglutinin, Limaxflavus.