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Issue 8, 2004
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Structure–activity relationships in aminocyclopentitol glycosidase inhibitors

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Abstract

Aminocyclopentitol analogs of β-D-glucose, β-D-galactose and α-D-galactose bearing alkyl substituents as aglycon mimics on the amine function were prepared and tested for inhibition of various glycosidases. N-benzyl-β-D-gluco derivatives 1–4 and N-benzyl-β-D-galacto derivative 5 inhibited β-galactosidase and β-glucosidase. N-benzyl-α-D-galacto aminocyclopentitol 6 strongly inhibited α-galactosidase. The inhibitory activities observed were generally stronger compared to those of their primary amine analogs. A structure–activity relationship analysis was carried out including data from thirty-five different aminocyclopentitol glycosidase inhibitors. The strongest inhibitions reported for any enzyme were associated with a perfect stereochemical match between aminocyclopentitol and glycosidase, including the α- or β-configuration of the amino-group corresponding to the enzyme's anomeric selectivity.

Graphical abstract: Structure–activity relationships in aminocyclopentitol glycosidase inhibitors

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Article information


Submitted
04 Dec 2003
Accepted
27 Feb 2004
First published
19 Mar 2004

Org. Biomol. Chem., 2004,2, 1217-1226
Article type
Paper

Structure–activity relationships in aminocyclopentitol glycosidase inhibitors

L. Gartenmann Dickson, E. Leroy and J. Reymond, Org. Biomol. Chem., 2004, 2, 1217
DOI: 10.1039/B315704K

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