alexa Delineating common molecular mechanisms in Alzheimer's and prion diseases.
Pharmaceutical Sciences

Pharmaceutical Sciences

Biochemistry & Pharmacology: Open Access

Author(s): Barnham KJ, Cappai R, Beyreuther K, Masters CL, Hill AF

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Abstract The structure of the infectious agent responsible for prion diseases has not been fully characterized, but evidence points to a beta-rich conformer of the host-encoded prion protein. Amyloid-beta peptide (Abeta), a proteolytic fragment generated from the amyloid precursor protein, has been implicated as the toxic molecule involved in the pathogenesis of Alzheimer's disease. The mechanism of Abeta toxicity might be mediated through the coordination of redox-active transition-metal ions such as copper leading to the generation of reactive oxygen species, coupled with the propensity to interact with lipid bilayers. Key sequence and chemical similarities between prion protein (PrP) and Abeta indicate that similar therapeutic strategies might be applicable for the treatment of Alzheimer's and prion diseases. This article was published in Trends Biochem Sci and referenced in Biochemistry & Pharmacology: Open Access

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