Stereoselective Synthesis of Boat‐Locked Glycosides Designed as Glycosyl Hydrolase Conformational Probes. Issue 7 (26th January 2015)

• Record Type: Journal Article
• Authors: Thiery, Emilie; Reniers, Jérémy; Wouters, Johan; Vincent, Stéphane P.
• Is Part Of: European journal of organic chemistry. Issue 7(2015)
• Page Start: 1472
• Page End: 1484
• Publication Date: 2015-01-26
• Subjects: Conformation analysis -- Carbohydrates -- Inhibitors -- Enzymes; Chemistry, Organic -- Periodicals; Organic compounds -- Synthesis -- Periodicals; Bioorganic chemistry -- Periodicals; Chemistry, Physical organic -- Periodicals; 547
• DOI: 10.1002/ejoc.201403363
• Languages: English
• ISSNs: 1434-193X

Abstract

Abstract: A general method for the preparation of galactose derivatives locked in a 1, 4 B boat conformation has been developed. The boat scaffold was stereoselectively functionalized at the C‐1′ position by aliphatic and aromatic groups along with azido or hydroxy groups. The configuration at the new stereogenic center was controlled and determined by X‐ray diffraction. These molecules were designed to probe the conformational itinerary of the substrate of glycosyl hydrolases. Inhibition assays were performed against a series of commercially available glycosidases, which showed that these enzymes do not harness a 1, 4 B ‐boat‐like transition state. Abstract : A general method for the preparation of galactose derivatives locked in a 1, 4 B boat conformation has been developed. The boat scaffold was stereoselectively functionalized at the C‐1′ position by aliphatic and aromatic groups along with azido or hydroxy groups. These molecules have been designed to probe the conformational itinerary of the substrate of glycosyl‐processing enzymes.