# The Effect of SARS-COV‑2 Protein Fragments on the Dimerization of α‑Synuclein

## TL;DR

This paper explores how fragments from the SARS-COV-2 virus may influence the formation of harmful protein structures linked to Parkinson’s Disease.

## Contribution

The study reveals how specific SARS-COV-2 protein fragments differentially stabilize α-synuclein dimers, potentially influencing fibril formation.

## Key findings

- Fragment FI10 from the spike protein and SK9 from the envelope protein stabilize α-synuclein dimers.
- These fragments preferentially seed rod-like fibrils over twister-like structures.
- Molecular dynamics simulations show differential stabilization effects.

## Abstract

There is evidence that amyloidogenic segments in SARS-COV-2
proteins
can induce aggregation of α-synuclein (αS), the main component
of brain-located amyloids whose presence is connected with Parkinson’s
Disease (PD). Using molecular dynamics simulations, we showed in earlier
work that SARS-COV-2 protein fragments shift the ensemble of αS
chains toward more aggregation-prone conformations. However, the mechanism
by which these chains assemble into fibrils, the presumed neurotoxic
agents in PD, is not clear. The first step on that route is the formation
of dimers. For this reason, we have now, using again molecular dynamics
simulations, studied how the fragment 194FKNIDGYFKI203 (FI10) of the SARS-COV-2 spike protein and the fragment 54SFYVYSRVK62 (SK9) of the envelope protein alter
the ensemble of α-synuclein dimers. Our simulations suggest
a differential stabilization of such dimers that would preferentially
seed rod-like fibrils over the competing twister-like structures.