Effect of an Amyloidogenic SARS-COV-2 Protein Fragment on α-Synuclein Monomers and Fibrils.
J Phys Chem B
; 126(20): 3648-3658, 2022 05 26.
Article
in English
| MEDLINE | ID: covidwho-1947182
ABSTRACT
Aggregates of α-synuclein are thought to be the disease-causing agent in Parkinson's disease. Various case studies have hinted at a correlation between COVID-19 and the onset of Parkinson's disease. For this reason, we use molecular dynamics simulations to study whether amyloidogenic regions in SARS-COV-2 proteins can initiate and modulate aggregation of α-synuclein. As an example, we choose the nine-residue fragment SFYVYSRVK (SK9), located on the C-terminal of the envelope protein of SARS-COV-2. We probe how the presence of SK9 affects the conformational ensemble of α-synuclein monomers and the stability of two resolved fibril polymorphs. We find that the viral protein fragment SK9 may alter α-synuclein amyloid formation by shifting the ensemble toward aggregation-prone and preferentially rod-like fibril seeding conformations. However, SK9 has only a small effect on the stability of pre-existing or newly formed fibrils. A potential mechanism and key residues for potential virus-induced amyloid formation are described.
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Parkinson Disease
/
Peptide Fragments
/
Alpha-Synuclein
/
Amyloidogenic Proteins
/
Coronavirus Envelope Proteins
Type of study:
Experimental Studies
Limits:
Humans
Language:
English
Journal:
J Phys Chem B
Journal subject:
Chemistry
Year:
2022
Document Type:
Article
Affiliation country:
Acs.jpcb.2c01254
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