Unprecedented Affinity Labeling of Carbohydrate-Binding Proteins with s -Triazinyl Glycosides

Arnaud Masselin (1) , Antoine Petrelli (1) , Maxime Donzel (1) , Sylvie Armand (1) , Sylvain Cottaz (1) , Sébastien Fort (1)

1 CERMAV - Centre de Recherches sur les Macromolécules Végétales

Carbohydrate–protein interactions trigger a wide range of biological signaling pathways, the mainstays of physiological and pathological processes. However, there are an incredible number of carbohydrate-binding proteins (CBPs) that remain to be identified and characterized. This study reports for the first time the covalent labeling of CBPs by triazinyl glycosides, a new and promising class of affinity-based glycoprobes. Mono- and bis-clickable triazinyl glycosides were efficiently synthesized from unprotected oligosaccharides (chitinpentaose and 2′-fucosyl-lactose) in a single step. These molecules allow the specific covalent labeling of chitin-oligosaccharide-binding proteins (wheat germ agglutinin WGA and Bc ChiA1 D202A, an inactivated chitinase) and fucosyl-binding lectin (UEA-I), respectively.

Domaines: Chimie thérapeutique; Biochimie, Biologie Moléculaire

Arnaud Masselin, Antoine Petrelli, Maxime Donzel, Sylvie Armand, Sylvain Cottaz, et al.. Unprecedented Affinity Labeling of Carbohydrate-Binding Proteins with s -Triazinyl Glycosides. Bioconjugate Chemistry, 2019, 30 (9), pp.2332-2339. ⟨10.1021/acs.bioconjchem.9b00432⟩. ⟨hal-02316484⟩