Investigating the Role of Alpha-Synuclein in Parkinson's Disease: A Molecular Dynamics Study
Abstract
Parkinson's disease is a neurodegenerative disorder characterized by the misfolding and aggregation of alpha-synuclein, leading to dopamine neuron death and motor function impairment. Despite its significance, the molecular mechanisms underlying alpha-synuclein's role in Parkinson's disease remain poorly understood. This study employed molecular dynamics simulations to investigate the structural and dynamic properties of alpha-synuclein in its monomeric and aggregated forms. Our results reveal that alpha-synuclein's aggregation propensity is driven by specific residue interactions, leading to the formation of toxic oligomers. Furthermore, we identified key conformational changes associated with alpha-synuclein's misfolding, which may contribute to its neurotoxicity. Our findings provide new insights into the molecular mechanisms of alpha-synuclein's role in Parkinson's disease, highlighting potential therapeutic targets for disease modification.
Keywords
Alpha-synuclein, Parkinson's disease, Molecular dynamics simulations, Protein misfolding, Aggregation, Neurodegeneration, Therapeutic targets
Citations
IRE Journals:
Olahanmi Olatayo
"Investigating the Role of Alpha-Synuclein in Parkinson's Disease: A Molecular Dynamics Study" Iconic Research And Engineering Journals Volume 8 Issue 1 2024 Page 593-603
IEEE:
Olahanmi Olatayo
"Investigating the Role of Alpha-Synuclein in Parkinson's Disease: A Molecular Dynamics Study" Iconic Research And Engineering Journals, 8(1)
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