The last decades have witnessed a growing global burden of Alzheimer’s disease (AD). Evidence indicates that the onset and progression of AD is associated with β-amyloid (Aβ) peptide fibrillation. As such, there is a strong passion with discovering potent Aβ fibrillation inhibitors that can be developed into anti-amyloiddogenic agents for AD treatment. Current challenges that have arisen with this development involve with Aβ oligomer toxicity suppression and Blood Brain Barrier penetration capability. Considering most natural or biological events, one would observe that there is usually a “seed” to direct natural materials to assemble in response to a certain stimulation. Inspired by this, several materials or compounds, including nanoparticle, peptide or peptide mimics, and organic molecules, have been designed for the purpose of redirecting or impeding Aβ aggregation. Achieving these tasks requires comprehensive understanding on (1) initial Aβ assembly into insoluble deposits, (2) main concerns with fibrillation inhibition, and (3) current major methodologies to disrupt the aggregation. Herein, the objective of this review is to address these three areas, and enable the pathway for a promising therapeutic agent design for AD treatment.

中文翻译：

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制定合理的设计来调节β-淀粉样蛋白原纤化以治疗阿尔茨海默氏病

在过去的几十年中，全球范围内阿尔茨海默氏病（AD）的负担日益增加。有证据表明AD的发作和发展与β-淀粉样蛋白（Aβ）肽原纤化有关。因此，人们强烈希望发现有效的Aβ纤颤抑制剂，这些抑制剂可以发展成抗淀粉样蛋白生成剂用于AD治疗。这种发展带来的当前挑战涉及Aβ低聚物毒性抑制和血脑屏障渗透能力。考虑到大多数自然或生物事件，人们会观察到通常存在一种“种子”来引导自然材料响应某种刺激而组装。受此启发，几种材料或化合物，包括纳米粒子，肽或肽模拟物以及有机分子，已经设计用于重定向或阻止Aβ聚集的目的。实现这些任务需要对以下方面有全面的了解：（1）初始Aβ组装成不溶性沉积物；（2）抑制原纤维形成的主要问题；以及（3）当前破坏聚集的主要方法。本文中，本综述的目的是解决这三个领域，并为AD治疗的治疗药物设计提供可行的途径。