The Neuronal tau protein blocks in vitro fibrillation of the amyloid-beta (A beta) peptide at the oligomeric stage - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of the American Chemical Society Année : 2018

The Neuronal tau protein blocks in vitro fibrillation of the amyloid-beta (A beta) peptide at the oligomeric stage

Résumé

In Alzheimer's disease, amyloid-beta (A beta) plaques and tau neurofibrillary tangles are the two pathological hallmarks. The co-occurrence and combined reciprocal pathological effects of A beta and tau protein aggregation have been observed in animal models of the disease. However, the molecular mechanism of their interaction remain unknown. Using a variety of biophysical measurements, we here show that the native full-length tau protein solubilizes the A beta(40) peptide and prevents its fibrillation. The tau protein delays the amyloid fibrillation of the A beta(40) peptide at substoichiometric ratios, showing different binding affinities toward the different stages of the aggregated A beta(40) peptides. The A beta monomer structure remains random coil in the presence of tau, as observed by nuclear magnetic resonance (NMR), circular dichroism (CD) spectroscopy and photoinduced cross-linking methods. We propose a potential interaction mechanism for the influence of tau on A beta fibrillation.
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Dates et versions

hal-02154329 , version 1 (12-06-2019)

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Cecilia Wallin, Yoshitaka Hiruma, Sebastian K. T. S. Warmlander, Isabelle Huvent, Juri Jarvet, et al.. The Neuronal tau protein blocks in vitro fibrillation of the amyloid-beta (A beta) peptide at the oligomeric stage. Journal of the American Chemical Society, 2018, 140 (26), pp.8138-8146. ⟨10.1021/jacs.7b13623⟩. ⟨hal-02154329⟩
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