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Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model

ABB Business Services Sp. z o.o. ul. Żegańska 1, 04-713 Warszawa, Poland
ACK—Cyfronet AGH, Nawojki 11, 30-950 Kraków, Poland
Department of Bioinformatics and Telemedicine, Medical College, Jagiellonian University, Łazarza 16, 31-530 Kraków, Poland
Faculty of Physics, Astronomy and Applied Computer Science, Jagiellonian University, Łojasiewicza 11, 30-348 Kraków, Poland
Chair of Medical Biochemistry, Medical College, Jagiellonian University, Kopernika 7, 31-034 Kraków, Poland
Author to whom correspondence should be addressed.
Currently address: Schibsted Tech Polska Sp. z o. o. ul. Armii Krajowej 28, 30-150 Kraków, Poland.
Int. J. Mol. Sci. 2018, 19(10), 2910;
Received: 14 July 2018 / Revised: 12 September 2018 / Accepted: 20 September 2018 / Published: 25 September 2018
(This article belongs to the Section Molecular Biophysics)
Abnormal filamentous aggregates that are formed by tangled tau protein turn out to be classic amyloid fibrils, meeting all the 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. View Full-Text
Keywords: tau amyloid; Alzheimer’s disease; tauopathy tau amyloid; Alzheimer’s disease; tauopathy
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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.

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