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Synthesis of Glycodendrimers Based on a Sugar Scaffold Targeting the DC-SIGN Lectin

Session: 
PS1 Poster session 1 Odd numbers
Code: 
P31
Location (hall): 
Foyer
Start/end time: 
Monday, July 1, 2019 - 15:45 to 17:15
Laurent
Cattiaux

Laurent Cattiaux1, Vanessa Porkolab2, Franck Fieschi2, Jean-Maurice Mallet1

1Laboratoire des Biomolécules, Département de chimie, École normale supérieure, PSL Research University, Sorbonne Universités. Paris 06, CNRS, 24 rue Lhomond, PARIS, FRANCE, 2Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale, Avenue des Martyrs, GRENOBLE, FRANCE

DC-SIGN (Dendritic Cell-Specific Intercellular adhesion molecule-3-Grabbing Nonintegrin; CD209 antigen), a lectin present mainly on the surface of dendritic cells plays a relevant role in the efficacy of the immune system. This lectin strongly interacts with highly mannosylated and fucosylated cell membranes of some pathogens leading to internalization into the dendritic cell. Many research groups have devoted their efforts in recent years to the development of highly glycosylated structures targeting DC-SIGN. 

We validated a unique synthesis of highly glycosylated dendrimers built from a amino acid derived from methyl glucoside and activity of final conjugates for DC-sign CBL were measured with the Biacore technique and a strong cooperatively of the sugars was found [1].

References: 
  1. Cattiaux, L.; Porkolab, V.; Fieschi, F.; Mallet, J-M. New branched amino acids for high affinity dendrimeric DC-SIGN ligands. Bioorg. Med. Chem. 2018, 26, 1006-1015.
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