Investigating the Role of Alpha-Synuclein in Parkinson's Disease: A Molecular Dynamics Study

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@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},
  }