1357005-68-5Relevant academic research and scientific papers
Exploring the synthetic potency of the first furanothioglycoligase through original remote activation
Almendros, Melanie,Danalev, Dantcho,Franois-Heude, Marc,Loyer, Pascal,Legentil, Laurent,Nugier-Chauvin, Caroline,Daniellou, Richard,Ferrieres, Vincent
, p. 8371 - 8378 (2012/04/05)
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. The Royal Society of Chemistry 2011.
α-l-Arabinofuranosylated pyrrolidines as arabinanase inhibitors
Goddard-Borger, Ethan D.,Carapito, Raphael,Jeltsch, Jean-Marc,Phalip, Vincent,Stick, Robert V.,Varrot, Annabelle
supporting information; experimental part, p. 9684 - 9686 (2011/10/09)
As part of continued efforts to understand the mechanisms of 1,5-α-l-arabinanases better, some arabinan-like iminosugar oligosaccharides were synthesized. An iminosugar analogue of arabinobiose was found to be a good inhibitor of the arabinanase Arb93A fr
