Preprint Article Version 1 This version is not peer-reviewed

Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria

Version 1 : Received: 14 July 2018 / Approved: 16 July 2018 / Online: 16 July 2018 (10:49:49 CEST)

A peer-reviewed article of this Preprint also exists.

Dułak, D.; Gadzała, M.; Banach, M.; Ptak, M.; Wiśniowski, Z.; Konieczny, L.; Roterman, I. Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model. Int. J. Mol. Sci. 2018, 19, 2910. Dułak, D.; Gadzała, M.; Banach, M.; Ptak, M.; Wiśniowski, Z.; Konieczny, L.; Roterman, I. Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model. Int. J. Mol. Sci. 2018, 19, 2910.

Journal reference: Int. J. Mol. Sci. 2018, 19, 2910
DOI: 10.3390/ijms19102910

Abstract

Abnormal filamentous aggregates formed by tangled tau protein turn out to be classic amyloid fibrils, meeting all criteria defined under the fuzzy oil drop model in the context of amyloid characterization. The model recognizes amyloids as linear structures where local hydrophobicity minima and maxima propagate in an alternating manner along the fibril’s long axis. This distribution of hydrophobicity differs greatly from the classic monocentric hydrophobic core observed in globular proteins. Rather than becoming a globule, the amyloid instead forms a ribbonlike (or cylindrical) structure, which can be thought of as a distorted spherical micelle, which in limit form appears to be the ribbon-like micelle.

Subject Areas

tau protein amyloids; Alzheimer’s disease; tauopathy

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