Specific Peptide from the Novel W-Tau Isoform Inhibits Tau and Amyloid β Peptide Aggregation In Vitro

[Image: see text] 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-...

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Autores principales: Cuadros, Raquel, Pérez, Mar, Ruiz-Gabarre, Daniel, Hernández, Félix, García-Escudero, Vega, Avila, Jesús
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2022
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9264359/
https://www.ncbi.nlm.nih.gov/pubmed/35695727
http://dx.doi.org/10.1021/acschemneuro.2c00188
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author Cuadros, Raquel
Pérez, Mar
Ruiz-Gabarre, Daniel
Hernández, Félix
García-Escudero, Vega
Avila, Jesús
author_facet Cuadros, Raquel
Pérez, Mar
Ruiz-Gabarre, Daniel
Hernández, Félix
García-Escudero, Vega
Avila, Jesús
author_sort Cuadros, Raquel
collection PubMed
description [Image: see text] 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.
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spelling pubmed-92643592022-07-09 Specific Peptide from the Novel W-Tau Isoform Inhibits Tau and Amyloid β Peptide Aggregation In Vitro Cuadros, Raquel Pérez, Mar Ruiz-Gabarre, Daniel Hernández, Félix García-Escudero, Vega Avila, Jesús ACS Chem Neurosci [Image: see text] 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. American Chemical Society 2022-06-13 /pmc/articles/PMC9264359/ /pubmed/35695727 http://dx.doi.org/10.1021/acschemneuro.2c00188 Text en © 2022 The Authors. Published by American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Cuadros, Raquel
Pérez, Mar
Ruiz-Gabarre, Daniel
Hernández, Félix
García-Escudero, Vega
Avila, Jesús
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
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_short 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
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9264359/
https://www.ncbi.nlm.nih.gov/pubmed/35695727
http://dx.doi.org/10.1021/acschemneuro.2c00188
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