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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.


Subject(s)
Amyloidogenic Proteins , Coronavirus Envelope Proteins , Parkinson Disease , Peptide Fragments , alpha-Synuclein , Amyloidogenic Proteins/chemistry , Amyloidogenic Proteins/metabolism , COVID-19/virology , Coronavirus Envelope Proteins/chemistry , Coronavirus Envelope Proteins/metabolism , Humans , Parkinson Disease/metabolism , Peptide Fragments/chemistry , Peptide Fragments/metabolism , SARS-CoV-2/metabolism , alpha-Synuclein/chemistry , alpha-Synuclein/metabolism
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