Beta-Amyloid (Aß) peptides are generated as cleavage products the Amyloid Precursor Protein (APP) by two proteases, ß-secretase and γ-secretase and are thought to be the causative agent (Shankar et al. Nature Medicine) in Alzheimer’s . Aßs are amphiphilic peptides with a hydrophilic N-terminal domain (residues 1 to 28) and a hydrophobic C-terminal (residues 29 to 42). The C-terminal domain corresponds to a portion of the transmembrane domain of APP. Heterogeneity at both ends of the peptides is known to affect the toxicity of beta-amyloid peptides. Amyloid deposits are insoluble and the core component of these plaques are Aß peptides that are 39 to 42 amino acid residues in length with a molecular mass of approximately 4 kDa (Olsson et al. Journal of Biological Chemistry). The most common peptide isoforms are Aβ40 and Aβ42 and early-onset Alzheimer’s is correlated with an increased production of Aβ42 relative to Aβ40 (Roher et al. PNAS).
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