SARS-COV-2 Spike Protein Fragment eases Amyloidogenesis of α-Synuclein

Parkinson’s Disease is accompanied by presence of amyloids in the brain formed of α-synuclein chains. Correlation between COVID-19 and the onset of Parkinson’s disease let to the idea that amyloidogenic segments in SARS-COV-2 proteins can induce aggregation of α-synuclein. Using molecular dynamic si...

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Autores principales: Chesney, Andrew D., Maiti, Buddhadev, Hansmann, Ulrich H. E.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory 2023
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10197603/
https://www.ncbi.nlm.nih.gov/pubmed/37214999
http://dx.doi.org/10.1101/2023.05.06.539715
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author Chesney, Andrew D.
Maiti, Buddhadev
Hansmann, Ulrich H. E.
author_facet Chesney, Andrew D.
Maiti, Buddhadev
Hansmann, Ulrich H. E.
author_sort Chesney, Andrew D.
collection PubMed
description Parkinson’s Disease is accompanied by presence of amyloids in the brain formed of α-synuclein chains. Correlation between COVID-19 and the onset of Parkinson’s disease let to the idea that amyloidogenic segments in SARS-COV-2 proteins can induce aggregation of α-synuclein. Using molecular dynamic simulations, we show that the fragment FKNIDGYFKI of the spike protein, which is unique for SARS-COV-2, shifts preferentially the ensemble of α-synuclein monomer towards rod-like fibril seeding conformations, and at the same time stabilizes differentially this polymorph over the competing twister-like structure. Our results are compared with earlier work relying on a different protein fragment that is not specific for SARS-COV-2.
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spelling pubmed-101976032023-05-20 SARS-COV-2 Spike Protein Fragment eases Amyloidogenesis of α-Synuclein Chesney, Andrew D. Maiti, Buddhadev Hansmann, Ulrich H. E. bioRxiv Article Parkinson’s Disease is accompanied by presence of amyloids in the brain formed of α-synuclein chains. Correlation between COVID-19 and the onset of Parkinson’s disease let to the idea that amyloidogenic segments in SARS-COV-2 proteins can induce aggregation of α-synuclein. Using molecular dynamic simulations, we show that the fragment FKNIDGYFKI of the spike protein, which is unique for SARS-COV-2, shifts preferentially the ensemble of α-synuclein monomer towards rod-like fibril seeding conformations, and at the same time stabilizes differentially this polymorph over the competing twister-like structure. Our results are compared with earlier work relying on a different protein fragment that is not specific for SARS-COV-2. Cold Spring Harbor Laboratory 2023-05-08 /pmc/articles/PMC10197603/ /pubmed/37214999 http://dx.doi.org/10.1101/2023.05.06.539715 Text en https://creativecommons.org/licenses/by-nc-nd/4.0/This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (https://creativecommons.org/licenses/by-nc-nd/4.0/) , which allows reusers to copy and distribute the material in any medium or format in unadapted form only, for noncommercial purposes only, and only so long as attribution is given to the creator.
spellingShingle Article
Chesney, Andrew D.
Maiti, Buddhadev
Hansmann, Ulrich H. E.
SARS-COV-2 Spike Protein Fragment eases Amyloidogenesis of α-Synuclein
title SARS-COV-2 Spike Protein Fragment eases Amyloidogenesis of α-Synuclein
title_full SARS-COV-2 Spike Protein Fragment eases Amyloidogenesis of α-Synuclein
title_fullStr SARS-COV-2 Spike Protein Fragment eases Amyloidogenesis of α-Synuclein
title_full_unstemmed SARS-COV-2 Spike Protein Fragment eases Amyloidogenesis of α-Synuclein
title_short SARS-COV-2 Spike Protein Fragment eases Amyloidogenesis of α-Synuclein
title_sort sars-cov-2 spike protein fragment eases amyloidogenesis of α-synuclein
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10197603/
https://www.ncbi.nlm.nih.gov/pubmed/37214999
http://dx.doi.org/10.1101/2023.05.06.539715
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