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

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 min...

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Autores principales: Dułak, Dawid, Gadzała, Małgorzata, Banach, Mateusz, Ptak, Magdalena, Wiśniowski, Zdzisław, Konieczny, Leszek, Roterman, Irena
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2018
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6213535/
https://www.ncbi.nlm.nih.gov/pubmed/30257460
http://dx.doi.org/10.3390/ijms19102910
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author Dułak, Dawid
Gadzała, Małgorzata
Banach, Mateusz
Ptak, Magdalena
Wiśniowski, Zdzisław
Konieczny, Leszek
Roterman, Irena
author_facet Dułak, Dawid
Gadzała, Małgorzata
Banach, Mateusz
Ptak, Magdalena
Wiśniowski, Zdzisław
Konieczny, Leszek
Roterman, Irena
author_sort Dułak, Dawid
collection PubMed
description 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.
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spelling pubmed-62135352018-11-14 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 Int J Mol Sci Article 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. MDPI 2018-09-25 /pmc/articles/PMC6213535/ /pubmed/30257460 http://dx.doi.org/10.3390/ijms19102910 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Dułak, Dawid
Gadzała, Małgorzata
Banach, Mateusz
Ptak, Magdalena
Wiśniowski, Zdzisław
Konieczny, Leszek
Roterman, Irena
Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model
title Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model
title_full Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model
title_fullStr Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model
title_full_unstemmed Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model
title_short Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model
title_sort filamentous aggregates of tau proteins fulfil standard amyloid criteria provided by the fuzzy oil drop (fod) model
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6213535/
https://www.ncbi.nlm.nih.gov/pubmed/30257460
http://dx.doi.org/10.3390/ijms19102910
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