Structural insights into copper and zinc binding to tau protein and the impact of metal binding on amyloid aggregation
Abstract
ions on the amyloid aggregation of full length Tau441 was evaluated using thioflavin T fluorescence, electrophoresis and transmission electron microscopy. Both metal ions significantly accelerate aggregation, promoting the formation of amyloid fibrils with distinct morphologies. Our study provides valuable structural insights into the copper and zinc binding sites in Tau441 that provide a rational basis to understand the impact of metal ions on amyloid fibril aggregation and morphology. The current study expands the bioinorganic facet of AD and other tauopathies, and it underscores the importance of metal-tau interactions as potential therapeutic targets in these neurodegenerative diseases.
Fields of Study & Subjects
Alzheimer's disease research and treatments
Trace Elements in Health
Aluminum toxicity and tolerance in plants and animals
Publication details
- Journal / source
- Chemical Science
- Publisher
- Royal Society of Chemistry (RSC)
- Volume
- 17
- Issue
- 14
- Pages
- 7277–7296
- Publication date
- 1 January 2026
- Language
- EN