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SARS-COV-2 Spike Protein Fragment eases Amyloidogenesis of α-Synuclein.


ABSTRACT: Parkinson's Disease is accompanied by presence of amyloids in the brain formed of α-synuclein chains. Correlation between COVID-19 and the onset of Parkinson's disease let 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, shifts preferentially the ensemble of α-synuclein monomer towards rod-like fibril seeding conformations, and at the same time stabilizes differentially 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.

SUBMITTER: Chesney AD 

PROVIDER: S-EPMC10197603 | biostudies-literature | 2023 May

REPOSITORIES: biostudies-literature

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SARS-COV-2 Spike Protein Fragment eases Amyloidogenesis of α-Synuclein.

Chesney Andrew D AD   Maiti Buddhadev B   Hansmann Ulrich H E UHE  

bioRxiv : the preprint server for biology 20230508


Parkinson's Disease is accompanied by presence of amyloids in the brain formed of α-synuclein chains. Correlation between COVID-19 and the onset of Parkinson's disease let 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, shifts preferentially the ensemble of α-synuclein monomer towards rod-like fibril seeding conforma  ...[more]

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