Molecular Profiles of Amyloid-β Proteoforms in Typical and Rapidly Progressive Alzheimer's Disease.

ABSTRACT: The molecular determinants of atypical clinical variants of Alzheimer's disease, including the recently discovered rapidly progressive Alzheimer's disease (rpAD), are unknown to date. Fibrilization of the amyloid-β (Aβ) peptide is the most frequently studied candidate in this context. The Aβ peptide can exist as multiple proteoforms that vary in their post-translational processing, amyloidogenesis, and toxicity. The current study was designed to identify these variations in Alzheimer's disease patients exhibiting classical (sAD) and rapid progression, with the primary aim of establishing if these variants may constitute strains that underlie the phenotypic variability of Alzheimer's disease. We employed two-dimensional polyacrylamide gel electrophoresis and MALDI-ToF mass spectrometry to v

SUBMITTER: Noor A 

PROVIDER: S-EPMC8786784 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature