Non-uniform self-assembly: On the anisotropic architecture of α-synuclein supra-fibrillar aggregates

Abstract Although the function of biopolymer hydrogels in nature depends on structural anisotropy at mesoscopic length scales, the self-assembly of such anisotropic structures in vitro is challenging. Here we show that fibrils of the protein α-synuclein spontaneously self-assemble into structurally...

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Autores principales:	Slav A. Semerdzhiev, Volodymyr V. Shvadchak, Vinod Subramaniam, Mireille M. A. E. Claessens
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/1596bfc132534431bae186e64f01ebf2
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spelling	oai:doaj.org-article:1596bfc132534431bae186e64f01ebf22021-12-02T16:06:49ZNon-uniform self-assembly: On the anisotropic architecture of α-synuclein supra-fibrillar aggregates10.1038/s41598-017-06532-12045-2322https://doaj.org/article/1596bfc132534431bae186e64f01ebf22017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-06532-1https://doaj.org/toc/2045-2322Abstract Although the function of biopolymer hydrogels in nature depends on structural anisotropy at mesoscopic length scales, the self-assembly of such anisotropic structures in vitro is challenging. Here we show that fibrils of the protein α-synuclein spontaneously self-assemble into structurally anisotropic hydrogel particles. While the fibrils in the interior of these supra-fibrillar aggregates (SFAs) are randomly oriented, the fibrils in the periphery prefer to cross neighboring fibrils at high angles. This difference in organization coincides with a significant difference in polarity of the environment in the central and peripheral parts of the SFA. We rationalize the structural anisotropy of SFAs in the light of the observation that αS fibrils bind a substantial amount of counterions. We propose that, with the progress of protein polymerization into fibrils, this binding of counterions changes the ionic environment which triggers a change in fibril organization resulting in anisotropy in the architecture of hydrogel particles.Slav A. SemerdzhievVolodymyr V. ShvadchakVinod SubramaniamMireille M. A. E. ClaessensNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Slav A. Semerdzhiev Volodymyr V. Shvadchak Vinod Subramaniam Mireille M. A. E. Claessens Non-uniform self-assembly: On the anisotropic architecture of α-synuclein supra-fibrillar aggregates
description	Abstract Although the function of biopolymer hydrogels in nature depends on structural anisotropy at mesoscopic length scales, the self-assembly of such anisotropic structures in vitro is challenging. Here we show that fibrils of the protein α-synuclein spontaneously self-assemble into structurally anisotropic hydrogel particles. While the fibrils in the interior of these supra-fibrillar aggregates (SFAs) are randomly oriented, the fibrils in the periphery prefer to cross neighboring fibrils at high angles. This difference in organization coincides with a significant difference in polarity of the environment in the central and peripheral parts of the SFA. We rationalize the structural anisotropy of SFAs in the light of the observation that αS fibrils bind a substantial amount of counterions. We propose that, with the progress of protein polymerization into fibrils, this binding of counterions changes the ionic environment which triggers a change in fibril organization resulting in anisotropy in the architecture of hydrogel particles.
format	article
author	Slav A. Semerdzhiev Volodymyr V. Shvadchak Vinod Subramaniam Mireille M. A. E. Claessens
author_facet	Slav A. Semerdzhiev Volodymyr V. Shvadchak Vinod Subramaniam Mireille M. A. E. Claessens
author_sort	Slav A. Semerdzhiev
title	Non-uniform self-assembly: On the anisotropic architecture of α-synuclein supra-fibrillar aggregates
title_short	Non-uniform self-assembly: On the anisotropic architecture of α-synuclein supra-fibrillar aggregates
title_full	Non-uniform self-assembly: On the anisotropic architecture of α-synuclein supra-fibrillar aggregates
title_fullStr	Non-uniform self-assembly: On the anisotropic architecture of α-synuclein supra-fibrillar aggregates
title_full_unstemmed	Non-uniform self-assembly: On the anisotropic architecture of α-synuclein supra-fibrillar aggregates
title_sort	non-uniform self-assembly: on the anisotropic architecture of α-synuclein supra-fibrillar aggregates
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/1596bfc132534431bae186e64f01ebf2
work_keys_str_mv	AT slavasemerdzhiev nonuniformselfassemblyontheanisotropicarchitectureofasynucleinsuprafibrillaraggregates AT volodymyrvshvadchak nonuniformselfassemblyontheanisotropicarchitectureofasynucleinsuprafibrillaraggregates AT vinodsubramaniam nonuniformselfassemblyontheanisotropicarchitectureofasynucleinsuprafibrillaraggregates AT mireillemaeclaessens nonuniformselfassemblyontheanisotropicarchitectureofasynucleinsuprafibrillaraggregates
_version_	1718384824822005760

Non-uniform self-assembly: On the anisotropic architecture of α-synuclein supra-fibrillar aggregates

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