Titre :

The Neuronal Tau Protein Blocks in Vitro Fibrillation of the Amyloid-β (Aβ) Peptide at the Oligomeric Stage

Auteur(s) :

Wallin, Cecilia [Auteur]
Stockholm University
Hiruma, Yoshitaka [Auteur]
Wärmländer, Sebastian K. T. S. [Auteur]
Stockholm University
Huvent, Isabelle [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Jarvet, Jüri [Auteur]
Stockholm University
Abrahams, Jan Pieter [Auteur]
Paul Scherrer Institute [PSI]
Gräslund, Astrid [Auteur]
Stockholm University
Lippens, Guy [Auteur]
Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés [LISBP]
Luo, Jinghui [Auteur]
Paul Scherrer Institute [PSI]

Titre de la revue :

Journal of the American Chemical Society

Date de publication :

2018-05-22

ISSN :

0002-7863, 1520-5126

Mot(s)-clé(s) en anglais :

Nanofibers
Peptides and proteins
Fluorescence
Oligomers
Aggregation

Discipline(s) HAL :

Chimie/Chimie théorique et/ou physique

Résumé en anglais : [en]

In Alzheimer’s disease, amyloid-β (Aβ) plaques and tau neurofibrillary tangles are the two pathological hallmarks. The co-occurrence and combined reciprocal pathological effects of Aβ and tau protein aggregation have been ...
Lire la suite >In Alzheimer’s disease, amyloid-β (Aβ) plaques and tau neurofibrillary tangles are the two pathological hallmarks. The co-occurrence and combined reciprocal pathological effects of Aβ 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 Aβ40 peptide and prevents its fibrillation. The tau protein delays the amyloid fibrillation of the Aβ40 peptide at substoichiometric ratios, showing different binding affinities toward the different stages of the aggregated Aβ40 peptides. The Aβ 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 Aβ fibrillation.Lire moins >

Langue :

Anglais

Audience :

Non spécifiée

Établissement(s) :

CNRS
Université de Lille

Collections :

• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Équipe(s) de recherche :

Chemical Glycobiology

Date de dépôt :

2020-02-12T15:45:06Z
2021-05-20T08:54:55Z