Tau Repeats Disassemble Amyloid-β Fibrils In Vitro by Interacting with KLVFFA and GGVVIA Domains
Abstract
The interplay between amyloid beta (Aβ) and tau protein is acknowledged as a crucial factor in the progression of Alzheimer's disease (AD), yet the precise molecular mechanisms underlying their interaction remain elusive. In this study, we explore how the key regions within tau, specifically the repeat domains, modulate Aβ aggregation. Through microscale thermophoresis and peptide mapping assays, we identified that tau repeats containing the amyloid motifs VQIINK and VQIVYK directly interact with Aβ(1-42) and Aβ(1-40), targeting the hydrophobic regions of Aβ. Tau repeats were found to inhibit Aβ fibril formation and promote the dissociation of preformed fibrils in vitro. Notably, while disassembling Aβ(1-42) fibrils, tau repeats concurrently stabilized oligomeric forms. These findings provide valuable insights into the complex mechanisms by which tau influences the Aβ pathology, with potential implications for AD progression.
Read the paper
Related studies
- Improving the translation of search strategies using the Polyglot Search Translator: a randomized controlled trial
- Nutritional, Physical, Cognitive, and Combination Interventions and Frailty Reversal Among Older Adults: A Randomized Controlled Trial
- Clinical characteristics and risk factors associated with COVID-19 severity in patients with haematological malignancies in Italy: a retrospective, multicentre, cohort study
- A randomized, controlled trial of oral propranolol in infantile hemangioma
- Clinical phenotypes of delirium during critical illness and severity of subsequent long-term cognitive impairment: a prospective cohort study
- Increased physical activity improves sleep and mood outcomes in inactive people with insomnia: a randomized controlled trial
Go deeper in Evidence Hub
Evidence Hub adds a study data sheet (design, sample size, evidence level, key numbers), an AI summary and a chat grounded in the paper's text.