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Understanding alpha-synuclein aggregation propensity in animals and humans

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  • معلومة اضافية
    • بيانات النشر:
      Elsevier, 2024.
    • الموضوع:
      2024
    • Collection:
      LCC:Biology (General)
      LCC:Biochemistry
    • نبذة مختصرة :
      Alpha-synuclein (α-syn) aggregation plays a critical role in the pathogenicity of Parkinson's Disease (PD). This study aims to evaluate the aggregation propensity of α-syn fragment peptides designed using the variability found in humans and animals. Thioflavin T (ThT) and transmission electron microscopy (TEM) were used to validate the formation of fibrils to identify important amino acid residues. Human α-syn fragments 51–75, 37–61, 62–86, 76–100, and 116–140 demonstrate a significantly higher tendency to aggregate compared to fragments 1–25, 26–50, and 91–115. All species analyzed of the α-syn 37–61 and 62–86 regions were shown to form fibrils on both ThT and TEM. The α-syn 37–61 and 62–86 fragment regions exhibited a high susceptibility to aggregation, with fibril formation observed in all species. The A53T mutation in several α-syn 37–61 fragments may enhance their propensity for aggregation, suggesting a correlation between this mutation and the capacity for fibril formation. Furthermore, the presence of the non-amyloid-β component (NAC) region, specifically in α-syn 62–86, was consistently observed in several fragments that displayed fibril formation, indicating a potential correlation between the NAC region and the process of fibril formation in α-syn. Finally, the combination of a high quantity of valine and a low quantity of acidic amino acids in these fragments may serve as indicators of α-syn fibril formation.
    • File Description:
      electronic resource
    • ISSN:
      2405-5808
    • Relation:
      http://www.sciencedirect.com/science/article/pii/S2405580824001742; https://doaj.org/toc/2405-5808
    • الرقم المعرف:
      10.1016/j.bbrep.2024.101810
    • الرقم المعرف:
      edsdoj.26834cd41672433e9d1c10ef63c1e9d2