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Investigating the Role of Alpha-Synuclein in Parkinson's Disease: A Molecular Dynamics Study
Subject area: Science,Engineering and Technology · Area of research: Chemistry
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
How to cite this paper
@article{1706099,
author = {Olahanmi Olatayo},
title = {Investigating the Role of Alpha-Synuclein in Parkinson's Disease: A Molecular Dynamics Study},
journal = {Iconic Research And Engineering Journals},
year = {2024},
volume = {8},
number = {1},
pages = {593-603},
issn = {2456-8880},
url = {https://www.irejournals.com/formatedpaper/1706099.pdf},
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},
month = {July},
}