Amyloid-β (Aβ) aggregation is recognized to be a key toxic factor in the pathogenesis of Alzheimer disease, which is the most common progressive neurodegenerative disorder. In vitro experiments have elucidated that Aβ aggregation depends on several factors, such as pH, temperature and peptide concentration. Despite the research effort in this field, the fundamental mechanism responsible for the disease progression is still unclear. Recent research has proposed the application of electric fields as a non-invasive therapeutic option leading to the disruption of amyloid fibrils. In this regard, a molecular level understanding of the interactions governing the destabilization mechanism represents an important research advancement. Understanding the electric field effects on proteins, provides a more in-depth comprehension of the relationship between protein conformation and electrostatic dipole moment.

The present study focuses on investigating the effect of static Electric Field (EF) on the conformational dynamics of Aβ fibrils by all-atom Molecular Dynamics (MD) simulations. The outcome of this work provides novel insight into this research field, demonstrating how the Aβ assembly may be destabilized by the applied EF.

淀粉样β（Aβ）聚集被认为是阿尔茨海默氏病发病机理中的关键毒性因子，该病是最常见的进行性神经退行性疾病。体外实验已经阐明，Aβ聚集取决于几个因素，例如pH，温度和肽浓度。尽管在该领域进行了研究，但尚不清楚导致疾病进展的基本机制。最近的研究提出了将电场作为导致淀粉样蛋白原纤维破裂的非侵入性治疗选择的应用。在这方面，从分子水平上理解控制不稳定机理的相互作用代表了重要的研究进展。了解电场对蛋白质的影响，

本研究的重点是通过全原子分子动力学（MD）模拟研究静态电场（EF）对Aβ原纤维构象动力学的影响。这项工作的成果为该研究领域提供了新颖的见解，证明了所应用的EF如何使Aβ组件不稳定。