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The Neuronal Tau Protein Blocks in Vitro Fibrillation of the Amyloid-beta (A beta) Peptide at the Oligomeric Stage
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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Number of Authors: 92018 (English)In: Journal of the American Chemical Society, ISSN 0002-7863, E-ISSN 1520-5126, Vol. 140, no 26, p. 8138-8146Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2018. Vol. 140, no 26, p. 8138-8146
National Category
Chemical Sciences
Research subject
Biophysics
Identifiers
URN: urn:nbn:se:su:diva-159116DOI: 10.1021/jacs.7b13623ISI: 000438309400018PubMedID: 29708745OAI: oai:DiVA.org:su-159116DiVA, id: diva2:1243877
Available from: 2018-08-31 Created: 2018-08-31 Last updated: 2020-05-20Bibliographically approved
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Wallin, CeciliaWärmländer, Sebastian K. T. S.Jarvet, JüriGräslund, AstridLippens, GuyLuo, Jinghui
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