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Effect of an Amyloidogenic SARS-COV-2 Protein Fragment on α-Synuclein Monomers and Fibrils.
Jana, Asis K; Lander, Chance W; Chesney, Andrew D; Hansmann, Ulrich H E.
  • Jana AK; Department of Chemistry & Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.
  • Lander CW; Department of Chemistry & Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.
  • Chesney AD; Department of Chemistry & Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.
  • Hansmann UHE; Department of Chemistry & Biochemistry, University of Oklahoma, Norman, Oklahoma 73019, United States.
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.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Parkinson Disease / Peptide Fragments / Alpha-Synuclein / Amyloidogenic Proteins / Coronavirus Envelope Proteins 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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Full text: Available Collection: International databases Database: MEDLINE Main subject: Parkinson Disease / Peptide Fragments / Alpha-Synuclein / Amyloidogenic Proteins / Coronavirus Envelope Proteins Limits: Humans Language: English Journal: J Phys Chem B Journal subject: Chemistry Year: 2022 Document Type: Article Affiliation country: Acs.jpcb.2c01254