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

Dułak, Dawid; Gadzała, Małgorzata; Banach, Mateusz; Ptak, Magdalena; Wiśniowski, Zdzisław; Konieczny, Leszek; Roterman, Irena

doi:10.3390/ijms19102910

Open AccessArticle

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

by

Dawid Dułak

¹,

Małgorzata Gadzała

^2,†,

Mateusz Banach

³

,

Magdalena Ptak

^3,4,

Zdzisław Wiśniowski

³,

Leszek Konieczny

⁵ and

Irena Roterman

^3,*

¹

ABB Business Services Sp. z o.o. ul. Żegańska 1, 04-713 Warszawa, Poland

²

ACK—Cyfronet AGH, Nawojki 11, 30-950 Kraków, Poland

³

Department of Bioinformatics and Telemedicine, Medical College, Jagiellonian University, Łazarza 16, 31-530 Kraków, Poland

⁴

Faculty of Physics, Astronomy and Applied Computer Science, Jagiellonian University, Łojasiewicza 11, 30-348 Kraków, Poland

⁵

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; https://doi.org/10.3390/ijms19102910

Submission received: 14 July 2018 / Revised: 12 September 2018 / Accepted: 20 September 2018 / Published: 25 September 2018

(This article belongs to the Section Molecular Biophysics)

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Abstract

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.

Keywords: tau amyloid; Alzheimer’s disease; tauopathy

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MDPI and ACS Style

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. https://doi.org/10.3390/ijms19102910

AMA Style

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. International Journal of Molecular Sciences. 2018; 19(10):2910. https://doi.org/10.3390/ijms19102910

Chicago/Turabian Style

Dułak, Dawid, Małgorzata Gadzała, Mateusz Banach, Magdalena Ptak, Zdzisław Wiśniowski, Leszek Konieczny, and Irena Roterman. 2018. "Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model" International Journal of Molecular Sciences 19, no. 10: 2910. https://doi.org/10.3390/ijms19102910

APA Style

Dułak, D., Gadzała, M., Banach, M., Ptak, M., Wiśniowski, Z., Konieczny, L., & Roterman, I. (2018). Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model. International Journal of Molecular Sciences, 19(10), 2910. https://doi.org/10.3390/ijms19102910

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

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