Jump to main content
Jump to site search

Issue 8, 2004
Previous Article Next Article

Structure–activity relationships in aminocyclopentitol glycosidase inhibitors

Author affiliations

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

Back to tab navigation

Publication details

The article was received on 04 Dec 2003, accepted on 27 Feb 2004 and first published on 19 Mar 2004


Article type: Paper
DOI: 10.1039/B315704K
Citation: Org. Biomol. Chem., 2004,2, 1217-1226
  •   Request permissions

    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

Search articles by author

Spotlight

Advertisements