bc9b00432_si_001.pdf (1.05 MB)
Unprecedented Affinity Labeling of Carbohydrate-Binding Proteins with s‑Triazinyl Glycosides
journal contribution
posted on 2019-08-23, 20:03 authored by Arnaud Masselin, Antoine Petrelli, Maxime Donzel, Sylvie Armand, Sylvain Cottaz, Sébastien FortCarbohydrate–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.
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carbohydrate-binding proteinscovalentTriazinylGlycosideaffinity-based glycoprobesbis-clickable triazinyl glycosidesfucosyl-binding lectinfucosyl-lactoseUnprecedented Affinitypathwaychitinpentaosemoleculemainstaychitinasechitin-oligosaccharide-binding proteinsMonotriazinyl glycosidesinteractionBc ChiA 1 D 202ACarbohydrate-Binding Proteinsstudy reportswheat germ agglutinin WGAUEA-ICBP
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