A robust preparation method for the amyloidogenic and intrinsically disordered amyloid-α peptide,Journal of Peptide Science

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A robust preparation method for the amyloidogenic and intrinsically disordered amyloid-α peptide
Journal of Peptide Science ( IF 1.8 ) Pub Date : 2022-04-28 , DOI: 10.1002/psc.3414
Ariel J Kuhn ₁ , Jevgenij A Raskatov ₁

Affiliation

Recent findings suggest that amyloid-β (Aβ) may not be the only peptidic culprit for the cognitive decline observed in patients with Alzheimer's disease. A C-terminal fragment of Aβ, amyloid-α (Aα), also known as p3, has been shown to form amyloidogenic oligomers and fibrils more rapidly than Aβ. However, the insolubility and aggregation propensity of this 24–26-residue peptide make it exceptionally difficult to produce, purify, and subsequently study. This paper reports a reproducible, multi-step method for the purification and pre-treatment of Aα and related analogues, yielding 95%–99% pure peptides. We anticipate that the methods described herein will permit previously inaccessible biophysical and biological experiments that may be critical to understanding the role of this too long overlooked peptide in AD disease pathology.

中文翻译：

一种稳定的淀粉样蛋白生成和本质无序淀粉样蛋白-α肽的制备方法

最近的研究结果表明，β 淀粉样蛋白 (Aβ) 可能不是导致阿尔茨海默病患者认知能力下降的唯一肽罪魁祸首。 Aβ 的 C 末端片段，淀粉样蛋白-α (Aα)，也称为 p3，已被证明比 Aβ 更快地形成淀粉样蛋白寡聚体和原纤维。然而，这种 24-26 个残基肽的不溶性和聚集倾向使其极其难以生产、纯化和随后的研究。本文报道了一种可重复的多步骤方法，用于纯化和预处理 Aα 及相关类似物，可产生 95%–99% 的纯肽。我们预计本文描述的方法将允许以前无法进行的生物物理和生物学实验，这对于理解这种长期被忽视的肽在 AD 疾病病理学中的作用可能至关重要。

更新日期：2022-04-28

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