Amyloid deposits are a hallmark of many diseases. In the case of Alzheimer's disease, a turn between 21Ala and 30Ala, stabilised by a salt bridge between 22Glu/23Asp and 28Lys, may nucleate folding and aggregation of the amyloid β (Aβ) peptide. In the present paper, we test this hypothesis by studying how salt bridge and turn formation vary with intrinsic and environmental changes, and how these changes affect folding and aggregation of the Aβ-peptide.

中文翻译：

---

内部和环境对阿尔茨海默病 β-淀粉样肽折叠和二聚化的影响

淀粉样蛋白沉积是许多疾病的标志。就阿尔茨海默病而言，21Ala 和 30Ala 之间的转折（通过 22Glu/23Asp 和 28Lys 之间的盐桥稳定）可能使 β 淀粉样蛋白 (Aβ) 肽的折叠和聚集成核。在本文中，我们通过研究盐桥和转角形成如何随内在和环境变化而变化，以及这些变化如何影响 Aβ 肽的折叠和聚集来检验这一假设。