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- W4308681937 abstract "The neurological symptoms of long COVID and viral neuroinvasion have raised concerns about the potential interactions between SARS-CoV-2 protein segments and neuronal proteins, which might confer a risk of post-infection neurodegeneration, but the underlying mechanisms remain unclear. Here, we reported that the receptor-binding domain (RBD) of the spike protein and the nine-residue segment (SK9) of the envelope protein could bind to α-synuclein (αSyn) with Kd values of 503 ± 24 nM and 12.7 ± 1.6 μM, respectively. RBD could inhibit αSyn fibrillization by blocking the non-amyloid-β component region and mediating its antiparallel β-sheet structural conversions. Omicron-RBD (BA.5) was shown to have a slightly stronger affinity for αSyn (Kd = 235 ± 10 nM), which implies similar effects, whereas SK9 may bind to the C-terminus which accelerates the formation of parallel β-sheet-containing oligomers and abruptly increases the rate of membrane disruption by 213%. Our results provide plausible molecular insights into the impact of SARS-CoV-2 post-infection and the oligomerization propensity of αSyn that is associated with Parkinson's disease." @default.
- W4308681937 created "2022-11-14" @default.
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- W4308681937 date "2022-11-10" @default.
- W4308681937 modified "2023-10-14" @default.
- W4308681937 title "Moderate Binding between Two SARS-CoV-2 Protein Segments and α-Synuclein Alters Its Toxic Oligomerization Propensity Differently" @default.
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- W4308681937 doi "https://doi.org/10.1021/acs.jpclett.2c02278" @default.
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