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 ( G0 2S 2 , G1 2S 2 and G2 2S 2 ) were used as Con A inhibitors and assayed by ELLA.