6-Azido d-galactose transfer to N-acetyl-d-glucosamine derivative using commercially available β-1,4-galactosyltransferase

Michaël Bosco (1) , Sophie Le Gall (2) , Christophe Rihouey (3) , Samuel Couve-Bonnaire (4) , Muriel Bardor (2) , Patrice Lerouge (2) , Xavier Pannecoucke (4)

1 IBMM - Institut des Biomolécules Max Mousseron [Pôle Chimie Balard]
2 GTCV - Glycobiologie et transports chez les végétaux
3 PBS - Polymères Biopolymères Surfaces
4 COBRA - Chimie Organique et Bioorganique : Réactivité et Analyse

A new strategy to tag glycoproteins carrying terminal GlcNAc was developed using commercially available bovine β-1,4-galactosyltransferase (GalT) and UDP-6-azidogalactose. The azide function was then allowed to react via a biotinylated Staudinger–Bertozzi probe demonstrating the usefulness of such a procedure to tag any glycoprotein possessing a N-acetylglucosamine terminal residue from any type of cell lysate.

Domains: Chemical Sciences; Catalysis; Chemical Sciences; Coordination chemistry; Chemical Sciences; Inorganic chemistry; Chemical Sciences; Organic chemistry; Chemical Sciences; Theoretical and/or physical chemistry; Chemical Sciences; Life Sciences [q-bio]; Biochemistry, Molecular Biology; Life Sciences [q-bio]; Cancer; Life Sciences [q-bio]

Michaël Bosco, Sophie Le Gall, Christophe Rihouey, Samuel Couve-Bonnaire, Muriel Bardor, et al.. 6-Azido d-galactose transfer to N-acetyl-d-glucosamine derivative using commercially available β-1,4-galactosyltransferase. Tetrahedron Letters, 2008, 49 (14), pp.2294-2297. ⟨10.1016/j.tetlet.2008.02.018⟩. ⟨hal-02384444⟩