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  1. Article: 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.

    Journal of physical chemistry. 2022 May 17, v. 126, no. 20

    2022  

    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 ... ...

    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.
    Keywords COVID-19 infection ; Severe acute respiratory syndrome coronavirus 2 ; amyloid ; etiological agents ; molecular dynamics
    Language English
    Dates of publication 2022-0517
    Size p. 3648-3658.
    Publishing place American Chemical Society
    Document type Article
    ISSN 1520-5207
    DOI 10.1021/acs.jpcb.2c01254
    Database NAL-Catalogue (AGRICOLA)

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  2. Article ; Online: 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

    The journal of physical chemistry. B

    2022  Volume 126, Issue 20, Page(s) 3648–3658

    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 ... ...

    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.
    MeSH term(s) 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
    Chemical Substances Amyloidogenic Proteins ; Coronavirus Envelope Proteins ; Peptide Fragments ; alpha-Synuclein ; envelope protein, SARS-CoV-2
    Language English
    Publishing date 2022-05-17
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural
    ISSN 1520-5207
    ISSN (online) 1520-5207
    DOI 10.1021/acs.jpcb.2c01254
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: 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

    bioRxiv : the preprint server for biology

    2022  

    Abstract: Using molecular dynamic simulations we study whether amyloidogenic regions in viral proteins can initiate and modulate formation of α-synuclein aggregates, thought to be the disease-causing agent in Parkinson's Disease. As an example we choose the nine- ... ...

    Abstract Using molecular dynamic simulations we study whether amyloidogenic regions in viral proteins can initiate and modulate formation of α-synuclein aggregates, thought to be the disease-causing agent in Parkinson's Disease. 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 little effect of the stability of pre-existing or newly-formed fibrils.
    Language English
    Publishing date 2022-02-23
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2022.02.21.481360
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  4. Article ; Online: 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.

    bioRxiv

    Abstract: Using molecular dynamic simulations we study whether amyloidogenic regions in viral proteins can initiate and modulate formation of alpha-synuclein aggregates, thought to be the disease-causing agent in Parkinson9s Disease. As an example we choose the ... ...

    Abstract Using molecular dynamic simulations we study whether amyloidogenic regions in viral proteins can initiate and modulate formation of alpha-synuclein aggregates, thought to be the disease-causing agent in Parkinson9s Disease. 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 alpha-synuclein monomers and the stability of two resolved fibril polymorphs. We find that the viral protein fragment SK9 may alter alpha-synuclein amyloid formation by shifting the ensemble toward aggregation-prone and preferentially rod-like fibril seeding conformations. However, SK9 has only little effect of the stability of pre-existing or newly-formed fibrils.
    Keywords covid19
    Language English
    Publishing date 2022-02-24
    Publisher Cold Spring Harbor Laboratory
    Document type Article ; Online
    DOI 10.1101/2022.02.21.481360
    Database COVID19

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