4.6 Article

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

Journal

ACS CHEMICAL NEUROSCIENCE
Volume -, Issue -, Pages -

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/acschemneuro.2c00188

Keywords

new tau isoform; w-Tau peptide; w-Tau peptide fragments; tau isoforms; amyloid peptide; aggregation

Funding

  1. Spanish Ministry of Science and Innovation [BES-2015-074405, PGC2018-096177-B-I00]
  2. Center for Networked Biomedical Research on Neurodegenerative Diseases
  3. Comunidad de Madrid [S2017/BMD]
  4. Fundacion Ramon Areces
  5. Banco de Santander

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W-Tau, a new human-specific splicing isoform, can inhibit the aggregation of tau and β-amyloid peptides through its unique 18-amino-acid sequence.
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 beta 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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