ArticlebioRxiv : the preprint server for biology2026
SEC Purified Monomeric Aβ42 Produces Reproducible and Reliable Aggregation Measurements.
Article in bioRxiv : the preprint server for biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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3 authors.
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Abstract
The accumulation of amyloid-beta (Aβ) plaques is a hallmark of Alzheimer's disease (AD), with Aβ42 representing the predominant and most aggregation-prone isoform. Reliable preparation of monomeric Aβ42 is essential for investigating the kinetics and mechanisms of its aggregation into oligomers and fibrils. This study provides a direct comparison of two monomerization protocols for recombinantly expressed Aβ42: one incorporating size-exclusion chromatography (SEC) and the other relying solely on chemical denaturation, using agents such as NaOH and NH
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