TOP > 新着情報 > The 29th Annual International Symposium on Computational Science and EngineeringよりANSCSE29 Poster Presentation Awardを受賞しました。(複雑系科学専攻 Prin Tadawattana D1)

The 29th Annual International Symposium on Computational Science and EngineeringよりANSCSE29 Poster Presentation Awardを受賞しました。(複雑系科学専攻 Prin Tadawattana D1)

  1. 受賞日：
  2. 受賞名：ANSCSE29 Poster Presentation Award
  3. 主催団体：The 29th Annual International Symposium on Computational Science and Engineering
  4. 受賞者の氏名、所属、職名（学年）：
    Prin Tadawattana (複雑系科学専攻 D1)
  5. 連名者：Toshifumi Mori・Norio Yoshida
  6. 受賞対象となった研究のテーマ：Elucidation of the Role of ATP in the Liquid-Liquid Phase Separation of α-synuclein
  7. 受賞概要：
    Parkinson’s disease (PD) and other synucleinopathies are associated with the liquid-liquid phase separation (LLPS) of α-synuclein into insoluble fibrils forming Lewy bodies (LBs) and Lewy neurites (LNs). Recent experimental studies have suggested that the liquid-to-solid transition of α-synuclein may involve the formation of amyloid-containing aggregates; however, the molecular understanding this process remains unclear. Herein, molecular dynamic (MD) simulations of five α-synuclein systems, ranging from monomer to pentamer, were performed for the NAC region were performed to investigate the oligomerization phenomena by evaluating the structural stability, intermolecular association, and residue-level interactions. The results indicate that the tetrameric assemblies exhibit transient oligomeric behavior, whereas the pentamer maintains a more persistent and dynamically stable intermolecular interactions throughout the simulation. Radius of gyration analysis shows that structural compactness of pentamer remains stable over time, suggesting that it retains relatively stable β-sheet characteristics based on secondary structure analysis. In addition, intermolecular contacts at the residue level reveal key interaction localized within the flexible disordered region (residues 18-28), implying that this segment may function as an important bridging region during oligomer formation. Overall, these findings propose that the early stages of α-synuclein oligomerization is influenced by oligomer size and dynamic intermolecular interactions within disordered regions, providing molecular insight into the initial aggregation process prior to mature fibril formation.

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