SARS-COV-2 Spike Protein Fragment eases Amyloidogenesis of α-Synuclein
Abstract
Parkinsons Disease is accompanied by presence of amyloids in the brain formed of -synuclein chains. Correlation between COVID-19 and the onset of Parkinsons disease let to the idea that amyloidogenic segments in SARS-COV-2 proteins can induce aggregation of -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 -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.
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