Scientists may have overlooked a hidden Alzheimer's culprit for decades — SkimNews
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- Jevgenij Raskatov published a commentary in ChemBioChem arguing that the P3 peptide, formed when Amyloid Precursor Protein is cut by α-secretase and γ-secretase, can form amyloid deposits and threadlike fibrils—often faster than the Aβ42 peptide blamed for Alzheimer's
- Raskatov's lab has published three major studies over the past five years showing P3 produces aggregates at least as readily as amyloid beta and may itself be neurotoxic, though less so than Aβ
- An independent UK research group has confirmed and expanded on the P3 findings, and other labs are now studying how P3 and amyloid beta interact in the brain
- Raskatov identified at least four peer-reviewed papers that cited his lab's work as evidence P3 was harmless, when his experiments had demonstrated the opposite, calling the citation pattern a 'grand confusion'
- UCLA emeritus professor David Teplow said the reevaluation has 'far-reaching consequences for both basic science and clinical research' into Alzheimer's causes and treatment
- Raskatov has proposed renaming P3 as 'Amyloid α' (Aα) to better reflect its aggregating ability and distinguish it from amyloid beta
- More than 400 Alzheimer's clinical trials have focused on amyloid beta, with many failing or producing only modest benefits; approved antibody drugs Lecanemab and Donanemab remove amyloid but have limited impact on disease progression
Why it matters: Alzheimer's affects roughly 35 million people and costs more than $800 billion annually, yet decades of amyloid-beta-focused drug development have produced limited results across 400-plus clinical trials. Raskatov's argument that P3 has been wrongly dismissed—and that respected journals cited his data backwards—opens a new drug-target lane and exposes a citation problem that may have steered the field off course for years.
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