Assessing reproducibility on Amyloid beta research: Impact of Abeta sources in experimental outcomes.

The difficulty to synthesize and purify the Amyloid beta (Abeta) peptide, combined with its high aggregation propensity and low solubility at physiological conditions, leads to a wide variety of experimental results from kinetic assays to biological activity. Thus, it becomes challenging to reproduce outcomes, which limits the ability to rely on reported results as the foundation for new research. This article examines variability of the Abeta 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 meaningful biophysical, biochemical, and neurobiological results can be obtained to improve our understanding on Abeta.