Atomic force microscopy imaging and nanomechanical properties of six Tau isoforms assemblies
Résumé
The aggregation of the protein tau is intimately associated with tauopathies such as Alzheimer’s disease. This study shows that the six different Tau isoforms form fibrils consisting of two protofibrils separated by a shallow groove. We show that Tau N-terminal inserts do not contribute to any morphological or mechanical difference among isoforms. Fibrils made of Tau molecules with four carboxyl‑terminal microtubule binding domains have a persistence length two-fold higher than those with three domains. The axial and radial Young’s moduli we determined are significantly lower than those of other amyloids suggesting weak intermolecular interaction between the paired β-sheets within Tau fibrils. The results show that Tau fibrils are labile, a property essential for their prion-like propagation propensity.
Domaines
BiophysiqueOrigine | Fichiers produits par l'(les) auteur(s) |
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