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: | , , , , , |
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| 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 |
| Sumario: | 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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