Journal
BIOCONJUGATE CHEMISTRY
Volume 30, Issue 9, Pages 2332-2339Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.bioconjchem.9b00432
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Funding
- Fondation pour le developpement de la chimie des substances naturelles et ses applications
- Labex ARCANE and CBH-EUR-GS [ANR-17-EURE-0003]
- Glyco@Alps [ANR-15-IDEX-02]
- PolyNat Carnot Institut [ANR-16-CARN-0025-01]
- ICMG [FR 2607]
- ANR NiceCrops [ANR-14-CE18-0008-01]
- Agence Nationale de la Recherche (ANR) [ANR-14-CE18-0008] Funding Source: Agence Nationale de la Recherche (ANR)
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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.
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