Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration

Protein aggregate formation is linked with multiple amyloidoses, including Alzheimer‘s and Parkinson‘s diseases. Currently, the understanding of such fibrillar structure formation and propagation is still not sufficient, the outcome of which is a lack of potent, anti-amyloid drugs. The environmental...

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Autores principales:	Mantas Ziaunys, Andrius Sakalauskas, Kamile Mikalauskaite, Vytautas Smirnovas
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	alpha-synuclein amyloid aggregation ionic strength polymorphism Biology (General) QH301-705.5 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/d66f5127a55743568622f55c7d58416f
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spelling	oai:doaj.org-article:d66f5127a55743568622f55c7d58416f2021-11-25T17:56:03ZPolymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration10.3390/ijms2222123821422-00671661-6596https://doaj.org/article/d66f5127a55743568622f55c7d58416f2021-11-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/22/12382https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067Protein aggregate formation is linked with multiple amyloidoses, including Alzheimer‘s and Parkinson‘s diseases. Currently, the understanding of such fibrillar structure formation and propagation is still not sufficient, the outcome of which is a lack of potent, anti-amyloid drugs. The environmental conditions used during in vitro protein aggregation assays play an important role in determining both the aggregation kinetic parameters, as well as resulting fibril structure. In the case of alpha-synuclein, ionic strength has been shown as a crucial factor in its amyloid aggregation. In this work, we examine a large sample size of alpha-synuclein aggregation reactions under thirty different ionic strength and protein concentration combinations and determine the resulting fibril structural variations using their dye-binding properties, secondary structure and morphology. We show that both ionic strength and protein concentration determine the structural variability of alpha-synuclein amyloid fibrils and that sometimes even identical conditions can result in up to four distinct types of aggregates.Mantas ZiaunysAndrius SakalauskasKamile MikalauskaiteVytautas SmirnovasMDPI AGarticlealpha-synucleinamyloidaggregationionic strengthpolymorphismBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 12382, p 12382 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	alpha-synuclein amyloid aggregation ionic strength polymorphism Biology (General) QH301-705.5 Chemistry QD1-999
spellingShingle	alpha-synuclein amyloid aggregation ionic strength polymorphism Biology (General) QH301-705.5 Chemistry QD1-999 Mantas Ziaunys Andrius Sakalauskas Kamile Mikalauskaite Vytautas Smirnovas Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration
description	Protein aggregate formation is linked with multiple amyloidoses, including Alzheimer‘s and Parkinson‘s diseases. Currently, the understanding of such fibrillar structure formation and propagation is still not sufficient, the outcome of which is a lack of potent, anti-amyloid drugs. The environmental conditions used during in vitro protein aggregation assays play an important role in determining both the aggregation kinetic parameters, as well as resulting fibril structure. In the case of alpha-synuclein, ionic strength has been shown as a crucial factor in its amyloid aggregation. In this work, we examine a large sample size of alpha-synuclein aggregation reactions under thirty different ionic strength and protein concentration combinations and determine the resulting fibril structural variations using their dye-binding properties, secondary structure and morphology. We show that both ionic strength and protein concentration determine the structural variability of alpha-synuclein amyloid fibrils and that sometimes even identical conditions can result in up to four distinct types of aggregates.
format	article
author	Mantas Ziaunys Andrius Sakalauskas Kamile Mikalauskaite Vytautas Smirnovas
author_facet	Mantas Ziaunys Andrius Sakalauskas Kamile Mikalauskaite Vytautas Smirnovas
author_sort	Mantas Ziaunys
title	Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration
title_short	Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration
title_full	Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration
title_fullStr	Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration
title_full_unstemmed	Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration
title_sort	polymorphism of alpha-synuclein amyloid fibrils depends on ionic strength and protein concentration
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/d66f5127a55743568622f55c7d58416f
work_keys_str_mv	AT mantasziaunys polymorphismofalphasynucleinamyloidfibrilsdependsonionicstrengthandproteinconcentration AT andriussakalauskas polymorphismofalphasynucleinamyloidfibrilsdependsonionicstrengthandproteinconcentration AT kamilemikalauskaite polymorphismofalphasynucleinamyloidfibrilsdependsonionicstrengthandproteinconcentration AT vytautassmirnovas polymorphismofalphasynucleinamyloidfibrilsdependsonionicstrengthandproteinconcentration
_version_	1718411834411712512

Polymorphism of Alpha-Synuclein Amyloid Fibrils Depends on Ionic Strength and Protein Concentration

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