Analyzing the electronic states and inter-/intra-molecular interactions of amyloid oligomers expand our understanding of the molecular basis of Alzheimer's disease and other amyloid diseases. In the current study, several high-resolution crystal structures of oligomeric assemblies of Aβ-derived peptides have been studied by the ab initio fragment molecular orbital (FMO) method. The FMO method provides comprehensive details of the molecular interactions between the residues of the amyloid oligomers at the quantum mechanical level. Based on the calculations, two sequential aromatic residues (F19 and F20) and negatively charged E22 on the central region of Aβ have been identified as key residues in oligomer stabilization and potential interesting pharmacophores for preventing oligomer formation.

中文翻译：

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基于大环β-发夹肽的片段分子轨道计算鉴定β-淀粉样蛋白寡聚体的关键稳定相互作用

分析淀粉样蛋白寡聚体的电子状态和分子间/分子内相互作用扩大了我们对阿尔茨海默病和其他淀粉样蛋白疾病分子基础的理解。在目前的研究中，已经通过从头算片段分子轨道 (FMO) 方法研究了A β衍生肽的寡聚组装体的几种高分辨率晶体结构。FMO 方法在量子力学水平上提供了淀粉样蛋白寡聚体残基之间分子相互作用的全面细节。根据计算，两个连续的芳香族残基（F19 和 F20）和带负电荷的 E22 在 A β的中心区域已被确定为低聚物稳定化的关键残基和用于防止低聚物形成的潜在有趣药效团。