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Does the SARS-CoV-2 Spike Receptor-Binding Domain Hamper the Amyloid Transformation of Alpha-Synuclein after All?

Biology

Does the SARS-CoV-2 Spike Receptor-Binding Domain Hamper the Amyloid Transformation of Alpha-Synuclein after All?

Y. Stroylova, A. Konstantinova, et al.

This groundbreaking research conducted by Yulia Stroylova and colleagues unveils an intriguing interaction between the SARS-CoV-2 spike protein's receptor-binding domain and alpha-synuclein, potentially linking COVID-19 to neurodegenerative processes. The study suggests that the receptor-binding domain may surprisingly inhibit alpha-synuclein amyloid transformation, reducing its cytotoxicity and hinting at new therapeutic avenues for Parkinson's disease.

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Playback language: English
Abstract
This study investigates the interaction between the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein and alpha-synuclein, a key protein in Parkinson's disease, to explore potential links between COVID-19 and neurodegenerative processes. Molecular modeling predicted a stable RBD-alpha-synuclein complex, confirmed immunochemically. Spectral analysis revealed interaction without secondary structure changes. Importantly, the RBD significantly inhibited alpha-synuclein amyloid transformation, and the resulting fibrils showed reduced cytotoxicity. This suggests that the RBD may not exacerbate, but rather mitigate, alpha-synuclein amyloid aggregation.
Publisher
Biomedicines
Published On
Feb 09, 2023
Authors
Yulia Stroylova, Anastasiia Konstantinova, Victor Stroylov, Ivan Katrukha, Fedor Rozov, Vladimir Muronetz
Tags
SARS-CoV-2
alpha-synuclein
Parkinson's disease
amyloid aggregation
neurodegeneration
molecular modeling
cytotoxicity
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