Moderate Binding between Two SARS-CoV-2 Protein Segments and α-Synuclein Alters Its Toxic Oligomerization Propensity Differently
Vince St. Dollente Mesias, Hongni Zhu, Xiao Tang, Xin Dai, Wei Liu, Yusong Guo, Jinqing Huang
Abstract
= 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.
Topics & Concepts
NeurodegenerationAlpha-synucleinAntiparallel (mathematics)ChemistryBiophysicsSpike ProteinBiologyCoronavirus disease 2019 (COVID-19)Parkinson's diseaseDiseaseMedicinePhysicsMagnetic fieldQuantum mechanicsPathologyInfectious disease (medical specialty)Long-Term Effects of COVID-19Neuroscience and Neural EngineeringNeuroinflammation and Neurodegeneration Mechanisms