Tuning glycosidase inhibition through aglycone interactions: Pharmacological chaperones for Fabry disease and GM 1 gangliosidosis

M. Aguilar-Moncayo, T. Takai, K. Higaki, T. Mena-Barragán, Y. Hirano, Kei 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

41 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 sp 2-iminosugars. Selected compounds were profiled as potent pharmacological chaperones for mutant lysosomal α- and β-Gal associated with Fabry disease and GM 1 gangliosidosis.

Original languageEnglish
Pages (from-to)6514-6516
Number of pages3
JournalChemical Communications
Volume48
Issue number52
DOIs
Publication statusPublished - 2012 Jul 4
Externally publishedYes

Fingerprint

Galactosidases
Glycoside Hydrolases
Tuning

ASJC Scopus subject areas

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

Cite this

Tuning glycosidase inhibition through aglycone interactions : Pharmacological chaperones for Fabry disease and GM 1 gangliosidosis. / Aguilar-Moncayo, M.; Takai, T.; Higaki, K.; Mena-Barragán, T.; Hirano, Y.; Yura, Kei; 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.

In: Chemical Communications, Vol. 48, No. 52, 04.07.2012, p. 6514-6516.

Research output: Contribution to journalArticle

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 GM 1 gangliosidosis', Chemical Communications, vol. 48, no. 52, pp. 6514-6516. https://doi.org/10.1039/c2cc32065g
Aguilar-Moncayo, M. ; Takai, T. ; Higaki, K. ; Mena-Barragán, T. ; Hirano, Y. ; Yura, Kei ; 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. / Tuning glycosidase inhibition through aglycone interactions : Pharmacological chaperones for Fabry disease and GM 1 gangliosidosis. In: Chemical Communications. 2012 ; Vol. 48, No. 52. pp. 6514-6516.
@article{374c8ddba19f48dfa0e8608b2c359913,
title = "Tuning glycosidase inhibition through aglycone interactions: Pharmacological chaperones for Fabry disease and GM 1 gangliosidosis",
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 sp 2-iminosugars. Selected compounds were profiled as potent pharmacological chaperones for mutant lysosomal α- and β-Gal associated with Fabry disease and GM 1 gangliosidosis.",
author = "M. Aguilar-Moncayo and T. Takai and K. Higaki and T. Mena-Barrag{\'a}n and Y. Hirano and Kei Yura and L. Li and Y. Yu and H. Ninomiya and Garc{\'i}a-Moreno, {M. I.} and S. Ishii and Y. Sakakibara and K. Ohno and E. Nanba and {Ortiz Mellet}, C. and {Garc{\'i}a Fern{\'a}ndez}, {J. M.} and Y. Suzuki",
year = "2012",
month = "7",
day = "4",
doi = "10.1039/c2cc32065g",
language = "English",
volume = "48",
pages = "6514--6516",
journal = "Chemical Communications",
issn = "1359-7345",
publisher = "Royal Society of Chemistry",
number = "52",

}

TY - JOUR

T1 - Tuning glycosidase inhibition through aglycone interactions

T2 - Pharmacological chaperones for Fabry disease and GM 1 gangliosidosis

AU - Aguilar-Moncayo, M.

AU - Takai, T.

AU - Higaki, K.

AU - Mena-Barragán, T.

AU - Hirano, Y.

AU - Yura, Kei

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.

PY - 2012/7/4

Y1 - 2012/7/4

N2 - 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 sp 2-iminosugars. Selected compounds were profiled as potent pharmacological chaperones for mutant lysosomal α- and β-Gal associated with Fabry disease and GM 1 gangliosidosis.

AB - 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 sp 2-iminosugars. Selected compounds were profiled as potent pharmacological chaperones for mutant lysosomal α- and β-Gal associated with Fabry disease and GM 1 gangliosidosis.

UR - http://www.scopus.com/inward/record.url?scp=84862156347&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84862156347&partnerID=8YFLogxK

U2 - 10.1039/c2cc32065g

DO - 10.1039/c2cc32065g

M3 - Article

C2 - 22618082

AN - SCOPUS:84862156347

VL - 48

SP - 6514

EP - 6516

JO - Chemical Communications

JF - Chemical Communications

SN - 1359-7345

IS - 52

ER -