Department of Chemistry and Biochemistry, University of California Santa Cruz, 1156 High Street, Santa Cruz, CA, 95064, USA.
Chembiochem. 2020 Sep 1;21(17):2425-2430. doi: 10.1002/cbic.202000125. Epub 2020 May 5.
The difficulty of synthesizing and purifying the amyloid β (Aβ) peptide, combined with its high aggregation propensity and low solubility under physiological conditions, leads to a wide variety of experimental results from kinetic assays to biological activity. Thus, it becomes challenging to reproduce outcomes, and this limits our ability to rely on reported results as the foundation for new research. This article examines variability of the Aβ peptide from different sources, comparing purity, and oligomer and fibril formation propensity side by side. The results highlight the importance of performing rigorous controls so that meaningful biophysical, biochemical, and neurobiological results can be obtained to improve our understanding on Aβ.
由于淀粉样β（Aβ）肽的合成和纯化难度较大，加上其在生理条件下具有很高的聚集倾向和低溶解度，导致从动力学测定到生物活性的各种实验结果差异很大。因此，难以重现结果，这限制了我们依赖已发表的结果作为新研究基础的能力。本文从不同来源比较了 Aβ 肽的变异性，比较了纯度、寡聚体和纤维形成倾向。结果强调了进行严格控制的重要性，以便获得有意义的生物物理、生物化学和神经生物学结果，从而提高我们对 Aβ 的理解。
