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The Neuronal Tau Protein Blocks in Vitro Fibrillation of the Amyloid-β (Aβ) Peptide at the Oligomeric Stage
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 4479725
Author(s) Wallin, Cecilia; Hiruma, Yoshitaka; Wärmländer, Sebastian K. T. S.; Huvent, Isabelle; Jarvet, Jüri; Abrahams, Jan Pieter; Gräslund, Astrid; Lippens, Guy; Luo, Jinghui
Author(s) at UniBasel Abrahams, Jan Pieter
Year 2018
Title The Neuronal Tau Protein Blocks in Vitro Fibrillation of the Amyloid-β (Aβ) Peptide at the Oligomeric Stage
Journal Journal of the American Chemical Society
Pages / Article-Number 8138-8146
Abstract 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 Aβ; 40; peptide and prevents its fibrillation. The tau protein delays the amyloid fibrillation of the Aβ; 40; peptide at substoichiometric ratios, showing different binding affinities toward the different stages of the aggregated Aβ; 40; 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.
ISSN/ISBN 1520-5126
edoc-URL https://edoc.unibas.ch/75788/
Full Text on edoc No
Digital Object Identifier DOI 10.1021/jacs.7b13623
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/29708745
 
   

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