Neuroscience · Scientific Reports 2025

α-Synuclein amyloids degrade ATP · 3D

3D 機制動畫:依照論文分鏡呈現核心生物機制。3D mechanism animation: the paper's core biological mechanism shown from the storyboard.
  1. 特寫單個 α-突觸核蛋白鏈在神經環境中發生錯誤摺疊,並自組裝成緻密的螺旋狀類澱粉纖維。
  2. 在細胞質中漂浮且發光的 ATP 分子,被類澱粉纖維表面規律的化學溝槽與活性位點捕捉。
  3. 結合在纖維表面的 ATP 分子化學鍵斷裂,釋放出失去原有亮度且色澤黯淡的較小 ADP 與 AMP 分子。
  4. 隨著內部能量耗盡,背景的多巴胺神經元變得灰暗透明,僅留下深色且僵硬的類澱粉纖維結構。
  1. Close-up of individual alpha-synuclein protein chains misfolding and self-assembling into a dense, spiraling amyloid fibril within a neural environment
  2. Glow-emitting ATP molecules floating in the cytoplasm are captured by the ordered chemical grooves and active sites on the surface of the alpha-synuclein amyloid fibril
  3. Chemical bonds of the bound ATP molecules break apart at the fibril surface, releasing smaller ADP and AMP molecules that lose their bright luminescence and turn dull
  4. The background dopaminergic neuron turns grey and translucent as its internal energy stores vanish, leaving behind the dark, rigid structure of the growing amyloid fibrils
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Castillo-Cáceres, C. et al. Alpha-synuclein amyloids catalyze nucleotide degradation. Scientific Reports (2025).

DOI: 10.1038/s41598-025-32888-w · 閱讀全文 →Read full text →

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