Synthesis of multimeric pyrrolidine iminosugar inhibitors of human β-glucocerebrosidase and α-galactosidase A: First example of a multivalent enzyme activity enhancer for Fabry disease

The synthesis of a chemical library of multimeric pyrrolidine-based iminosugars by incorporation of three pairs of epimeric pyrrolidine-azides into different alkyne scaffolds via CuAAC is presented. The new multimers were evaluated as inhibitors of two important therapeutic enzymes, human α-galactos...

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Autores: Martínez Bailén, Macarena, Carmona Asenjo, Ana Teresa, Cardona, Francesca, Matassini, Camilla, Goti, Andrea, Kubo, Moemi, Kato, Atsushi, Robina Ramírez, Inmaculada, Moreno Vargas, Antonio José
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2020
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/176972
Acceso en línea:https://hdl.handle.net/11441/176972
https://doi.org/10.1016/j.ejmech.2020.112173
Access Level:acceso abierto
Palabra clave:Iminosugars
Multivalency
Glycosidases
α-galactosidase inhibitors
βglucocerebrosidase inhibitors
Pharmacological chaperones
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spelling Synthesis of multimeric pyrrolidine iminosugar inhibitors of human β-glucocerebrosidase and α-galactosidase A: First example of a multivalent enzyme activity enhancer for Fabry diseaseMartínez Bailén, MacarenaCarmona Asenjo, Ana TeresaCardona, FrancescaMatassini, CamillaGoti, AndreaKubo, MoemiKato, AtsushiRobina Ramírez, InmaculadaMoreno Vargas, Antonio JoséIminosugarsMultivalencyGlycosidasesα-galactosidase inhibitorsβglucocerebrosidase inhibitorsPharmacological chaperonesThe synthesis of a chemical library of multimeric pyrrolidine-based iminosugars by incorporation of three pairs of epimeric pyrrolidine-azides into different alkyne scaffolds via CuAAC is presented. The new multimers were evaluated as inhibitors of two important therapeutic enzymes, human α-galactosidase A (α-Gal A) and lysosomal β-glucocerebrosidase (GCase). Structure-activity relationships were established focusing on the iminosugar inhitope, the valency of the dendron and the linker between the inhitope and the central scaffold. Remarkable is the result obtained in the inhibition of α-Gal A, where one of the nonavalent compounds showed potent inhibition (0.20 μM, competitive inhibition), being a 375-fold more potent inhibitor than the monovalent reference. The potential of the best α-Gal A inhibitors to act as pharmacological chaperones was analyzed by evaluating their ability to increase the activity of this enzyme in R301G fibroblasts from patients with Fabry disease, a genetic disorder related with a reduced activity of α-Gal A. The best enzyme activity enhancement was obtained for the same nonavalent compound, which increased 5.2-fold the activity of the misfolded enzyme at 2.5 μM, what constitutes the first example of a multivalent α-Gal A activity enhancer of potential interest in the treatment of Fabry disease.ElsevierQuímica OrgánicaMinisterio de Economía y Competitividad (MINECO). EspañaJunta de AndalucíaJapanese Society for the Promotion of ScienceEnte Cassa di Risparmio di Firenze2020info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/176972https://doi.org/10.1016/j.ejmech.2020.112173reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésEuropean Journal of Medicinal Chemistry, 192, 112173.CTQ2016-77270-RFQM-345JP17K083622016/08452018.0942https://doi.org/10.1016/j.ejmech.2020.112173info:eu-repo/semantics/openAccessoai:idus.us.es:11441/1769722026-06-17T12:51:07Z
dc.title.none.fl_str_mv Synthesis of multimeric pyrrolidine iminosugar inhibitors of human β-glucocerebrosidase and α-galactosidase A: First example of a multivalent enzyme activity enhancer for Fabry disease
title Synthesis of multimeric pyrrolidine iminosugar inhibitors of human β-glucocerebrosidase and α-galactosidase A: First example of a multivalent enzyme activity enhancer for Fabry disease
spellingShingle Synthesis of multimeric pyrrolidine iminosugar inhibitors of human β-glucocerebrosidase and α-galactosidase A: First example of a multivalent enzyme activity enhancer for Fabry disease
Martínez Bailén, Macarena
Iminosugars
Multivalency
Glycosidases
α-galactosidase inhibitors
βglucocerebrosidase inhibitors
Pharmacological chaperones
title_short Synthesis of multimeric pyrrolidine iminosugar inhibitors of human β-glucocerebrosidase and α-galactosidase A: First example of a multivalent enzyme activity enhancer for Fabry disease
title_full Synthesis of multimeric pyrrolidine iminosugar inhibitors of human β-glucocerebrosidase and α-galactosidase A: First example of a multivalent enzyme activity enhancer for Fabry disease
title_fullStr Synthesis of multimeric pyrrolidine iminosugar inhibitors of human β-glucocerebrosidase and α-galactosidase A: First example of a multivalent enzyme activity enhancer for Fabry disease
title_full_unstemmed Synthesis of multimeric pyrrolidine iminosugar inhibitors of human β-glucocerebrosidase and α-galactosidase A: First example of a multivalent enzyme activity enhancer for Fabry disease
title_sort Synthesis of multimeric pyrrolidine iminosugar inhibitors of human β-glucocerebrosidase and α-galactosidase A: First example of a multivalent enzyme activity enhancer for Fabry disease
dc.creator.none.fl_str_mv Martínez Bailén, Macarena
Carmona Asenjo, Ana Teresa
Cardona, Francesca
Matassini, Camilla
Goti, Andrea
Kubo, Moemi
Kato, Atsushi
Robina Ramírez, Inmaculada
Moreno Vargas, Antonio José
author Martínez Bailén, Macarena
author_facet Martínez Bailén, Macarena
Carmona Asenjo, Ana Teresa
Cardona, Francesca
Matassini, Camilla
Goti, Andrea
Kubo, Moemi
Kato, Atsushi
Robina Ramírez, Inmaculada
Moreno Vargas, Antonio José
author_role author
author2 Carmona Asenjo, Ana Teresa
Cardona, Francesca
Matassini, Camilla
Goti, Andrea
Kubo, Moemi
Kato, Atsushi
Robina Ramírez, Inmaculada
Moreno Vargas, Antonio José
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Química Orgánica
Ministerio de Economía y Competitividad (MINECO). España
Junta de Andalucía
Japanese Society for the Promotion of Science
Ente Cassa di Risparmio di Firenze
dc.subject.none.fl_str_mv Iminosugars
Multivalency
Glycosidases
α-galactosidase inhibitors
βglucocerebrosidase inhibitors
Pharmacological chaperones
topic Iminosugars
Multivalency
Glycosidases
α-galactosidase inhibitors
βglucocerebrosidase inhibitors
Pharmacological chaperones
description The synthesis of a chemical library of multimeric pyrrolidine-based iminosugars by incorporation of three pairs of epimeric pyrrolidine-azides into different alkyne scaffolds via CuAAC is presented. The new multimers were evaluated as inhibitors of two important therapeutic enzymes, human α-galactosidase A (α-Gal A) and lysosomal β-glucocerebrosidase (GCase). Structure-activity relationships were established focusing on the iminosugar inhitope, the valency of the dendron and the linker between the inhitope and the central scaffold. Remarkable is the result obtained in the inhibition of α-Gal A, where one of the nonavalent compounds showed potent inhibition (0.20 μM, competitive inhibition), being a 375-fold more potent inhibitor than the monovalent reference. The potential of the best α-Gal A inhibitors to act as pharmacological chaperones was analyzed by evaluating their ability to increase the activity of this enzyme in R301G fibroblasts from patients with Fabry disease, a genetic disorder related with a reduced activity of α-Gal A. The best enzyme activity enhancement was obtained for the same nonavalent compound, which increased 5.2-fold the activity of the misfolded enzyme at 2.5 μM, what constitutes the first example of a multivalent α-Gal A activity enhancer of potential interest in the treatment of Fabry disease.
publishDate 2020
dc.date.none.fl_str_mv 2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/11441/176972
https://doi.org/10.1016/j.ejmech.2020.112173
url https://hdl.handle.net/11441/176972
https://doi.org/10.1016/j.ejmech.2020.112173
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv European Journal of Medicinal Chemistry, 192, 112173.
CTQ2016-77270-R
FQM-345
JP17K08362
2016/0845
2018.0942
https://doi.org/10.1016/j.ejmech.2020.112173
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
repository.mail.fl_str_mv
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