Cargando…

WT and A53T α-Synuclein Systems: Melting Diagram and Its New Interpretation

The potential barriers governing the motions of α-synuclein (αS) variants’ hydration water, especially energetics of them, is in the focus of the work. The thermodynamical approach yielded essential information about distributions and heights of the potential barriers. The proteins’ structural disor...

Descripción completa

Detalles Bibliográficos
Autores principales: Bokor, Mónika, Tantos, Ágnes, Tompa, Péter, Han, Kyou-Hoon, Tompa, Kálmán
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7312601/
https://www.ncbi.nlm.nih.gov/pubmed/32503167
http://dx.doi.org/10.3390/ijms21113997
_version_ 1783549766964084736
author Bokor, Mónika
Tantos, Ágnes
Tompa, Péter
Han, Kyou-Hoon
Tompa, Kálmán
author_facet Bokor, Mónika
Tantos, Ágnes
Tompa, Péter
Han, Kyou-Hoon
Tompa, Kálmán
author_sort Bokor, Mónika
collection PubMed
description The potential barriers governing the motions of α-synuclein (αS) variants’ hydration water, especially energetics of them, is in the focus of the work. The thermodynamical approach yielded essential information about distributions and heights of the potential barriers. The proteins’ structural disorder was measured by ratios of heterogeneous water-binding interfaces. They showed the αS monomers, oligomers and amyloids to possess secondary structural elements, although monomers are intrinsically disordered. Despite their disordered nature, monomers have 33% secondary structure, and therefore they are more compact than a random coil. At the lowest potential barriers with mobile hydration water, monomers are already functional, a monolayer of mobile hydration water is surrounding them. Monomers realize all possible hydrogen bonds with the solvent water. αS oligomers and amyloids have half of the mobile hydration water amount than monomers because aggregation involves less mobile hydration. The solvent-accessible surface of the oligomers is ordered or homogenous in its interactions with water to 66%. As a contrast, αS amyloids are disordered or heterogeneous to 75% of their solvent accessible surface and both wild type and A53T amyloids show identical, low-level hydration. Mobile water molecules in the first hydration shell of amyloids are the weakest bound compared to other forms.
format Online
Article
Text
id pubmed-7312601
institution National Center for Biotechnology Information
language English
publishDate 2020
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-73126012020-06-29 WT and A53T α-Synuclein Systems: Melting Diagram and Its New Interpretation Bokor, Mónika Tantos, Ágnes Tompa, Péter Han, Kyou-Hoon Tompa, Kálmán Int J Mol Sci Article The potential barriers governing the motions of α-synuclein (αS) variants’ hydration water, especially energetics of them, is in the focus of the work. The thermodynamical approach yielded essential information about distributions and heights of the potential barriers. The proteins’ structural disorder was measured by ratios of heterogeneous water-binding interfaces. They showed the αS monomers, oligomers and amyloids to possess secondary structural elements, although monomers are intrinsically disordered. Despite their disordered nature, monomers have 33% secondary structure, and therefore they are more compact than a random coil. At the lowest potential barriers with mobile hydration water, monomers are already functional, a monolayer of mobile hydration water is surrounding them. Monomers realize all possible hydrogen bonds with the solvent water. αS oligomers and amyloids have half of the mobile hydration water amount than monomers because aggregation involves less mobile hydration. The solvent-accessible surface of the oligomers is ordered or homogenous in its interactions with water to 66%. As a contrast, αS amyloids are disordered or heterogeneous to 75% of their solvent accessible surface and both wild type and A53T amyloids show identical, low-level hydration. Mobile water molecules in the first hydration shell of amyloids are the weakest bound compared to other forms. MDPI 2020-06-03 /pmc/articles/PMC7312601/ /pubmed/32503167 http://dx.doi.org/10.3390/ijms21113997 Text en © 2020 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
Bokor, Mónika
Tantos, Ágnes
Tompa, Péter
Han, Kyou-Hoon
Tompa, Kálmán
WT and A53T α-Synuclein Systems: Melting Diagram and Its New Interpretation
title WT and A53T α-Synuclein Systems: Melting Diagram and Its New Interpretation
title_full WT and A53T α-Synuclein Systems: Melting Diagram and Its New Interpretation
title_fullStr WT and A53T α-Synuclein Systems: Melting Diagram and Its New Interpretation
title_full_unstemmed WT and A53T α-Synuclein Systems: Melting Diagram and Its New Interpretation
title_short WT and A53T α-Synuclein Systems: Melting Diagram and Its New Interpretation
title_sort wt and a53t α-synuclein systems: melting diagram and its new interpretation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7312601/
https://www.ncbi.nlm.nih.gov/pubmed/32503167
http://dx.doi.org/10.3390/ijms21113997
work_keys_str_mv AT bokormonika wtanda53tasynucleinsystemsmeltingdiagramanditsnewinterpretation
AT tantosagnes wtanda53tasynucleinsystemsmeltingdiagramanditsnewinterpretation
AT tompapeter wtanda53tasynucleinsystemsmeltingdiagramanditsnewinterpretation
AT hankyouhoon wtanda53tasynucleinsystemsmeltingdiagramanditsnewinterpretation
AT tompakalman wtanda53tasynucleinsystemsmeltingdiagramanditsnewinterpretation