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Assessing Reproducibility in Amyloid β Research: Impact of Aβ Sources on Experimental Outcomes
Author(s) -
Foley Alejandro R.,
Raskatov Jevgenij A.
Publication year - 2020
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202000125
Subject(s) - peptide , oligomer , amyloid (mycology) , amyloid β , biochemical engineering , chemistry , computational biology , computer science , biophysics , biological system , biochemistry , biology , medicine , engineering , inorganic chemistry , disease , organic chemistry
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.