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, Y. Suzuki

Research output: Contribution to journalArticle

43 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)6514-6516
Number of pages3
JournalChemical Communications
Volume48
Issue number52
DOIs
Publication statusPublished - 2012 Jun 6

ASJC Scopus subject areas

  • Catalysis
  • Electronic, Optical and Magnetic Materials
  • Ceramics and Composites
  • Chemistry(all)
  • Surfaces, Coatings and Films
  • Metals and Alloys
  • Materials Chemistry

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  • Cite this

    Aguilar-Moncayo, M., Takai, T., Higaki, K., Mena-Barragán, T., Hirano, Y., Yura, K., Li, L., Yu, Y., Ninomiya, H., García-Moreno, M. I., Ishii, S., Sakakibara, Y., Ohno, K., Nanba, E., Ortiz Mellet, C., García Fernández, J. M., & Suzuki, Y. (2012). Tuning glycosidase inhibition through aglycone interactions: Pharmacological chaperones for Fabry disease and GM1 gangliosidosis. Chemical Communications, 48(52), 6514-6516. https://doi.org/10.1039/c2cc32065g