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

• Published in: Bioconjugate chemistry Vol. 30; no. 9; pp. 2332 - 2339
• Main Authors: Masselin, Arnaud, Petrelli, Antoine, Donzel, Maxime, Armand, Sylvie, Cottaz, Sylvain, Fort, Sébastien
• Format: Journal Article
• Language: English
• Published: WASHINGTON American Chemical Society 18.09.2019; Amer Chemical Soc
• Subjects: Affinity; Affinity labeling; Binding; Biochemical Research Methods; Biochemistry & Molecular Biology; Carbohydrates; Chemical Sciences; Chemistry; Chemistry, Multidisciplinary; Chemistry, Organic; Chitin; Chitinase; Glycosides; Labeling; Lactose; Life Sciences; Life Sciences & Biomedicine; Medicinal Chemistry; Oligosaccharide-binding proteins; Oligosaccharides; Physical Sciences; Protein interaction; Proteins; Science & Technology; Wheat; Wheat germ; Wheat germ agglutinin; PHOTOAFFINITY PROBES; OLIGOSACCHARIDES; N-ACETYLCHITOHEXAOSE; CHITINASE A1; IDENTIFICATION; PHOTOPROBES; DERIVATIVES; RESIDUES; SYMBIOSIS; CHLORIDE
• ISSN: 1043-1802; 1520-4812
• DOI: 10.1021/acs.bioconjchem.9b00432

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.