Jump to main content
Jump to site search

Issue 52, 2012
Previous Article Next Article

Tuning glycosidase inhibition through aglycone interactions: pharmacological chaperones for Fabry disease and GM1 gangliosidosis

Author affiliations

Abstract

Competitive inhibitors of either α-galactosidase (α-Gal) or β-galactosidase (β-Gal) with high affinity and selectivity have been accessed by exploiting aglycone interactions with conformationally locked sp2-iminosugars. Selected compounds were profiled as potent pharmacological chaperones for mutant lysosomal α- and β-Gal associated with Fabry disease and GM1 gangliosidosis.

Graphical abstract: Tuning glycosidase inhibition through aglycone interactions: pharmacological chaperones for Fabry disease and GM1 gangliosidosis

Back to tab navigation

Supplementary files

Article information


Submitted
21 Mar 2012
Accepted
08 May 2012
First published
09 May 2012

Chem. Commun., 2012,48, 6514-6516
Article type
Communication

Tuning glycosidase inhibition through aglycone interactions: pharmacological chaperones for Fabry disease and GM1 gangliosidosis

M. Aguilar-Moncayo, T. Takai, K. Higaki, T. Mena-Barragán, Y. Hirano, K. Yura, L. Li, Y. Yu, H. Ninomiya, M. I. García-Moreno, S. Ishii, Y. Sakakibara, K. Ohno, E. Nanba, C. Ortiz Mellet, J. M. García Fernández and Y. Suzuki, Chem. Commun., 2012, 48, 6514
DOI: 10.1039/C2CC32065G

Social activity

Search articles by author

Spotlight

Advertisements