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...
| Autores: | , , , , , |
|---|---|
| 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 |
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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 |
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Biblos-e Archivo. Repositorio Institucional de la UAM |
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15.300724 |