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Significance Amyloid β (Aβ) aggregation has been the therapeutic target of several Alzheimer’s disease (AD) clinical trials. Aβ exists in many different aggregated forms, making it exceedingly challenging to target. Evidence links intracellular Aβ accumulation and AD pathogenesis. We report that amino acids 1 to 30 of Aβ, Aβ (1–30), do not aggregate yet display cellular uptake stereospecificity when compared to its mirror image, suggesting that Aβ uptake is predominantly receptor-mediated and may be independent from its aggregation state. Additionally, we found Aβ (1–30) internalization to depend on PrPC expression. Aβ (1–30) thus represents a powerful tool to study mechanisms of Aβ cellular internalization and suggests that Aβ uptake could be modulated by therapeutically targeting high-affinity Aβ receptors.

Evidence for aggregation-independent, PrP C -mediated Aβ cellular internalization

Evidence for aggregation-independent, PrP ^C -mediated Aβ cellular internalization