Synthesis of glycopeptide dendrimers, dimerization and affinity for Concanavalin A

We described herein the synthesis of second generation glycopeptide dendrimers G2a–g presenting variable amino acids placed internally into the multivalent scaffold. The effect of such structural modulation on recognition processes by Concanavalin A (Con A), was then estimated by enhanced-sensitivity Enzyme-Linked Lectin Assay (ELLA). In a complementary study, glycopeptide dendrons of different valencies and including a l-cysteine residue before the dendritic core (G0SH, G1SH and G2SH), were also synthesized and homodimerized. Then, the disulfide-containing glycopeptide dendrimers generated by this convergent approach (G02S2, G12S2 and G22S2) were used as Con A inhibitors and assayed by ELLA.

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