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Abstract: 3,6-Anhydro-1-(aryl or alkylamino)-1-deoxy-d-sorbitol derivatives have been prepared in four steps from isosorbide, a by-product from the starch industry. The inhibitory activities of these new compounds have been evaluated towards 13 glycosidases. A first lead-compound was identified, which inhibited β-N-acetylglucosaminidase from bovine kidney (82% inhibition at 1mM). [Copyright &y& Elsevier]

[Display omitted] • Protecting-group-free synthesis of glycoconjugates. • Cycloadditions under Microwave activation. • Strong antifungal isoxazolidines obtained in good yields and few steps. • Potential use as crop-protecting agents. A straightforward synthesis of carbohydrate templated isoxazolidines is described, by reaction of unprotected glycosylhydroxylamines (operating as 1,3-dipoles) with methyl acrylate using microwave activation. Rhamno - and erythro -isoxazolidines are recognized by plant cells, resulting in a strong ROS-production as a plant immune response, and exert a high antifungal activity against Botrytis cinerea. [ABSTRACT FROM AUTHOR]

A series of diastereomeric tetrahydroxylated azepanes featuring a carboxymethyl group at the pseudo-anomeric position have been synthesized from a common unsaturated intermediate. Syn - and anti -dihydroxylation reactions were achieved to yield the target compounds after efficient one-step deprotection of carbamate, ester and acetonide groups simultaneously. Screening of these polyhydroxylated azepanes toward a range of commercially available glycosidases was performed and one of the stereoisomers showed potent and selective inhibition toward β-galactosidase (IC 50 = 21 μM). [ABSTRACT FROM AUTHOR]

[Display omitted] • Synthesis of a chromogenic analogue of myo -inositol hexaphosphate. • Amenable to g-scale. • Docking experiments confirmed the compatibility with the active site of phytases. • Phytases operate experimentally with this fluorogenic substrate. A new myo -inositol pentakisphosphate was synthesized, which featured a dansyl group at position C-5. The fluorescent tag was removed from the inositol by a 6-atom spacer to prevent detrimental steric interactions in the catalytic site of phytases. The PEG linker was used in order to enhance hydrophilicity and biocompatibility of the new artificial substrate. Computational studies showed a favorable positioning in the catalytic site of phytases. Enzymatic assays demonstrated that the tethered myo -inositol was processed by two recombinant phytases Phy-A and Phy-C, classified respectively as acid and alkaline phytases, with similar rates of phosphate release compared to their natural substrate. [ABSTRACT FROM AUTHOR]