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SARS-COV-2 spike protein fragment eases amyloidogenesis of α-synuclein.

Authors :
Chesney, Andrew D.
Maiti, Buddhadev
Hansmann, Ulrich H. E.
Source :
Journal of Chemical Physics. 7/7/2023, Vol. 159 Issue 1, p1-9. 9p.
Publication Year :
2023

Abstract

Parkinson's disease is accompanied by the presence of amyloids in the brain that are formed of α-synuclein chains. The correlation between COVID-19 and the onset of Parkinson's disease led 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, preferentially shifts the ensemble of α-synuclein monomer toward rod-like fibril seeding conformations and, at the same time, differentially stabilizes 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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00219606
Volume :
159
Issue :
1
Database :
Academic Search Index
Journal :
Journal of Chemical Physics
Publication Type :
Academic Journal
Accession number :
164785160
Full Text :
https://doi.org/10.1063/5.0157331