Specific peptide from the novel W-Tau isoform inhibits tau and amyloid β peptide aggregation in vitro

W-Tau, a new tau human-specific splicing isoform generated by intron retention, has been recently described. This isoform contains an 18-residue unique sequence corresponding to the translation of the retained region of intron 12. In this work, we have described that such 18-amino-acid peptide from...

Descripción completa

Detalles Bibliográficos
Autores: Cuadros, Raquel, Pérez Martínez, María Mar, Ruiz-Gabarre, Daniel, Hernández Pérez, Félix, García-Escudero Barreras, María Vega, Avila, Jesús
Tipo de recurso: artículo
Fecha de publicación:2022
País:España
Institución:Universidad Autónoma de Madrid
Repositorio:Biblos-e Archivo. Repositorio Institucional de la UAM
Idioma:inglés
OAI Identifier:oai:repositorio.uam.es:10486/705187
Acceso en línea:http://hdl.handle.net/10486/705187
https://dx.doi.org/10.1021/acschemneuro.2c00188
Access Level:acceso abierto
Palabra clave:aggregation
amyloid peptide
new tau isoform
tau isoforms
w-Tau peptide
w-Tau peptide fragments
Medicina
id ES_8a0dc0e37de49487bfbd7beca3b8ca58
oai_identifier_str oai:repositorio.uam.es:10486/705187
network_acronym_str ES
network_name_str España
repository_id_str
spelling Specific peptide from the novel W-Tau isoform inhibits tau and amyloid β peptide aggregation in vitroCuadros, RaquelPérez Martínez, María MarRuiz-Gabarre, DanielHernández Pérez, FélixGarcía-Escudero Barreras, María VegaAvila, Jesúsaggregationamyloid peptidenew tau isoformtau isoformsw-Tau peptidew-Tau peptide fragmentsMedicinaW-Tau, a new tau human-specific splicing isoform generated by intron retention, has been recently described. This isoform contains an 18-residue unique sequence corresponding to the translation of the retained region of intron 12. In this work, we have described that such 18-amino-acid peptide from the retained intron 12 can inhibit tau and β amyloid peptides aggregation under in vitro conditions. This inhibitory function is also present in smaller fragments of the 18-residue peptideThis research was funded by the Spanish Ministry of Science and Innovation (BES-2015-074405 and PGC2018-096177-BI00), the Center for Networked Biomedical Research on Neurodegenerative Diseases, and the Comunidad de Madrid (S2017/BMD). Institutional grants from the Fundación Ramón Areces and Banco de Santander are also acknowledged.American Chemical SocietyDepartamento de Anatomía, Histología y NeurocienciaFacultad de Medicina20222022-06-13research articlehttp://purl.org/coar/resource_type/c_2df8fbb1VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10486/705187https://dx.doi.org/10.1021/acschemneuro.2c00188reponame:Biblos-e Archivo. Repositorio Institucional de la UAMinstname:Universidad Autónoma de MadridInglésengopen accesshttp://purl.org/coar/access_right/c_abf2info:eu-repo/semantics/openAccessoai:repositorio.uam.es:10486/7051872026-06-23T12:46:27Z
dc.title.none.fl_str_mv Specific peptide from the novel W-Tau isoform inhibits tau and amyloid β peptide aggregation in vitro
title Specific peptide from the novel W-Tau isoform inhibits tau and amyloid β peptide aggregation in vitro
spellingShingle Specific peptide from the novel W-Tau isoform inhibits tau and amyloid β peptide aggregation in vitro
Cuadros, Raquel
aggregation
amyloid peptide
new tau isoform
tau isoforms
w-Tau peptide
w-Tau peptide fragments
Medicina
title_short Specific peptide from the novel W-Tau isoform inhibits tau and amyloid β peptide aggregation in vitro
title_full Specific peptide from the novel W-Tau isoform inhibits tau and amyloid β peptide aggregation in vitro
title_fullStr Specific peptide from the novel W-Tau isoform inhibits tau and amyloid β peptide aggregation in vitro
title_full_unstemmed Specific peptide from the novel W-Tau isoform inhibits tau and amyloid β peptide aggregation in vitro
title_sort Specific peptide from the novel W-Tau isoform inhibits tau and amyloid β peptide aggregation in vitro
dc.creator.none.fl_str_mv Cuadros, Raquel
Pérez Martínez, María Mar
Ruiz-Gabarre, Daniel
Hernández Pérez, Félix
García-Escudero Barreras, María Vega
Avila, Jesús
author Cuadros, Raquel
author_facet Cuadros, Raquel
Pérez Martínez, María Mar
Ruiz-Gabarre, Daniel
Hernández Pérez, Félix
García-Escudero Barreras, María Vega
Avila, Jesús
author_role author
author2 Pérez Martínez, María Mar
Ruiz-Gabarre, Daniel
Hernández Pérez, Félix
García-Escudero Barreras, María Vega
Avila, Jesús
author2_role author
author
author
author
author
dc.contributor.none.fl_str_mv Departamento de Anatomía, Histología y Neurociencia
Facultad de Medicina
dc.subject.none.fl_str_mv aggregation
amyloid peptide
new tau isoform
tau isoforms
w-Tau peptide
w-Tau peptide fragments
Medicina
topic aggregation
amyloid peptide
new tau isoform
tau isoforms
w-Tau peptide
w-Tau peptide fragments
Medicina
description W-Tau, a new tau human-specific splicing isoform generated by intron retention, has been recently described. This isoform contains an 18-residue unique sequence corresponding to the translation of the retained region of intron 12. In this work, we have described that such 18-amino-acid peptide from the retained intron 12 can inhibit tau and β amyloid peptides aggregation under in vitro conditions. This inhibitory function is also present in smaller fragments of the 18-residue peptide
publishDate 2022
dc.date.none.fl_str_mv 2022
2022-06-13
dc.type.none.fl_str_mv research article
http://purl.org/coar/resource_type/c_2df8fbb1
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10486/705187
https://dx.doi.org/10.1021/acschemneuro.2c00188
url http://hdl.handle.net/10486/705187
https://dx.doi.org/10.1021/acschemneuro.2c00188
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
dc.source.none.fl_str_mv reponame:Biblos-e Archivo. Repositorio Institucional de la UAM
instname:Universidad Autónoma de Madrid
instname_str Universidad Autónoma de Madrid
reponame_str Biblos-e Archivo. Repositorio Institucional de la UAM
collection Biblos-e Archivo. Repositorio Institucional de la UAM
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869412672371425280
score 15.300724