Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 110, Issue 4, Pages E313-E321Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1212100110
Keywords
protein aggregation; Alzheimer's disease; paired helical filaments
Categories
Funding
- M. DiFiglia and the Philly Dake EM center at the Massassachusetts General Hospital
- European Molecular Biology Organization
- Eidgenossiche Technische Hochschule
- Deutsche Forschungsgemeinschaft
- Max-Planck-Gesellschaft
- Deutsches Zentrum fur Neurodegenerative Erkrankungen
- Swiss National Science Foundation
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The structure and properties of amyloid-like Tau fibrils accumulating in neurodegenerative diseases have been debated for decades. Although the core of Tau fibrils assembles from short beta-strands, the properties of the much longer unstructured Tau domains protruding from the fibril core remain largely obscure. Applying immunogold transmission EM, and force-volume atomic force microscopy (AFM), we imaged human Tau fibrils at high resolution and simultaneously mapped their mechanical and adhesive properties. Tau fibrils showed a approximate to 16-nm-thick fuzzy coat that resembles a two-layered polyelectrolyte brush, which is formed by the unstructured short C-terminal and long N-terminal Tau domains. The mechanical and adhesive properties of the fuzzy coat are modulated by electrolytes and pH, and thus by the cellular environment. These unique properties of the fuzzy coat help in understanding how Tau fibrils disturb cellular interactions and accumulate in neurofibrillary tangles.
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