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

doi:10.1039/c2cc32065g

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

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

53 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 language	English
Pages (from-to)	6514-6516
Number of pages	3
Journal	Chemical Communications
Volume	48
Issue number	52
DOIs	https://doi.org/10.1039/c2cc32065g
Publication status	Published - 2012 Jun 6
Externally published	Yes

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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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

Aguilar-Moncayo, M, Takai, T, Higaki, K, Mena-Barragán, T, Hirano, Y, Yura, K, Li, L, Yu, Y, Ninomiya, H, García-Moreno, MI, Ishii, S, Sakakibara, Y, Ohno, K, Nanba, E, Ortiz Mellet, C, García Fernández, JM & Suzuki, Y 2012, 'Tuning glycosidase inhibition through aglycone interactions: Pharmacological chaperones for Fabry disease and GM₁ gangliosidosis', Chemical Communications, vol. 48, no. 52, pp. 6514-6516. https://doi.org/10.1039/c2cc32065g

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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.",

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AU - Takai, T.

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AU - Mena-Barragán, T.

AU - Hirano, Y.

AU - Yura, K.

AU - Li, L.

AU - Yu, Y.

AU - Ninomiya, H.

AU - García-Moreno, M. I.

AU - Ishii, S.

AU - Sakakibara, Y.

AU - Ohno, K.

AU - Nanba, E.

AU - Ortiz Mellet, C.

AU - García Fernández, J. M.

AU - Suzuki, Y.

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

Abstract

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