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 such a convergent approach (G02S2, G12S2 and G22S2) were used as Con A inhibitors and assaied by ELLA.


Published in:
Bioorganic and Medicinal Chemistry, 19, 9, 2879–2887
Year:
2011
Publisher:
Elsevier
ISSN:
0968-0896
Keywords:
Laboratories:




 Record created 2011-03-22, last modified 2018-03-17


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