Synthesis of glycopeptide dendrimers, dimerization and affinity for Concanavalin A.
Ronan Euzen, Jean-Louis Reymond
文献索引:Bioorg. Med. Chem. 19 , 2879-87, (2011)
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摘要
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(2)S(2), G1(2)S(2) and G2(2)S(2)) were used as Con A inhibitors and assayed by ELLA.Copyright © 2011 Elsevier Ltd. All rights reserved.
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