title: Synthesis of glycopeptide dendrimers, dimerization and affinity for Concanavalin A.
abstract: 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.
authors.affiliation: Technicians Training Laboratory, Institute of Chemical Sciences and Engineering (ISIC-GE), Ecole Polytechnique Fédérale de Lausanne, Lausanne CH-1015, Switzerland. ronan.euzen@epfl.ch
authors.forename: Ronan
authors.initials: R
authors.lastname: Euzen
authors.forename: Jean-Louis
authors.initials: JL
authors.lastname: Reymond
mesh_terms: D003208:Concanavalin A / Q000037:antagonists & inhibitors* / Q000378:metabolism; D050091:Dendrimers / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D019281:Dimerization; D006020:Glycopeptides / Q000138:chemical synthesis / Q000737:chemistry*
chemical_list: D050091:Dendrimers; D006020:Glycopeptides; D003208:Concanavalin A