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Article type: Review Article
Authors: Kuhn, Ariel J. | Raskatov, Jevgenij; *
Affiliations: Department of Chemistry and Biochemistry, University of California Santa Cruz, Physical Sciences Building, Santa Cruz, CA, USA
Correspondence: [*] Correspondence to: Jevgenij Raskatov, Department of Chemistry and Biochemistry, University of California Santa Cruz, Physical Sciences Building, 1156 High Street, Santa Cruz, CA 95064, USA. Tel.: 831 459 2978; E-mail: [email protected].
Note: [1] In memoriam Christopher M. Dobson.
Abstract: Despite the vast heterogeneity of amyloid plaques isolated from the brains of those with Alzheimer’s Disease (AD), the basis of the Amyloid Cascade Hypothesis targets a single peptide, the amyloid-β (Aβ) peptide. The countless therapeutic efforts targeting the production and aggregation of this specific peptide have been met with disappointment, leaving many to question the role of Aβ in AD. An alternative cleavage product of the Amyloid-β protein precursor, called the p3 peptide, which has also been isolated from the brains of AD patients, has been largely absent from most Aβ-related studies. Typically referred to as non-amyloidogenic and even suggested as neuroprotective, the p3 peptide has garnered little attention aside from some conflicting findings on cytotoxicity and potential self-assembly to form higher order aggregates. Herein, we report an extensive analysis of the findings surrounding p3 and offer some evidence as to why it may not be as innocuous as previously suggested.
Keywords: Amyloid-β, amyloids, intrinsically disordered proteins, p3, peptides
DOI: 10.3233/JAD-191201
Journal: Journal of Alzheimer's Disease, vol. 74, no. 1, pp. 43-53, 2020
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