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Issue 52, 2012
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Tuning glycosidase inhibition through aglycone interactions: pharmacological chaperones for Fabry disease and GM1 gangliosidosis

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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

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Publication details

The article was received on 21 Mar 2012, accepted on 08 May 2012 and first published on 09 May 2012


Article type: Communication
DOI: 10.1039/C2CC32065G
Citation: Chem. Commun., 2012,48, 6514-6516

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    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

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