Exploring the synthetic potency of the first furanothioglycoligase through original remote activation.

Mélanie Almendros (1) , Dantcho Danalev (1) , Marc François-Heude (1) , Pascal Loyer (2) , Laurent Legentil (1) , Caroline Nugier-Chauvin (1) , Richard Daniellou (1) , Vincent Ferrières (1)

1 ISCR - Institut des Sciences Chimiques de Rennes
2 Foie, métabolismes et cancer

Thioglycosidic bonds are of utmost importance in biomolecules as their incorporation led to more stable glycomimetics with potential drug activities. Until now only chemical methods were available for their incorporation into glycofuranosyl conjugates. Herein, we wish to describe the use of the first furanothioglycoligase for the preparation of a great variety of thioaryl derivatives with moderate to excellent yields. Of great interest, a stable 1-thioimidoyl arabinofuranose, classically used in chemical glycosylation, was able to efficiently act as a donor through an original enzymatic remote activation mechanism. Study of the chemical structure as well as the nucleophilicity of the thiol allowed us to optimize this biocatalyzed process. As a consequence, this mutated enzyme constitutes an original, mild and eco-friendly method of thioligation.

Domaines: Chimie organique

Mélanie Almendros, Dantcho Danalev, Marc François-Heude, Pascal Loyer, Laurent Legentil, et al.. Exploring the synthetic potency of the first furanothioglycoligase through original remote activation.. Organic & Biomolecular Chemistry, 2011, 9 (24), pp.8371-8. ⟨10.1039/c1ob06227a⟩. ⟨hal-00754558⟩