On the amyloid-β transcytosis across the blood–brain barrier

Abstract

The blood–brain barrier regulates the movement of misfolded proteins into and out of the central nervous system. LRP1 is one of the receptors doing that work, and it handles several misfolded proteins, amyloid-β among them.

We found that the barrier sorts large molecules by their affinity for LRP1. High-affinity cargo stays in the endocytic pathway; mid-affinity cargo travels in tubular vesicles held open by the BAR-domain protein syndapin-2.

We are now looking at other LRP receptors, LRP8 included, and building multivalent polymeric nanoparticles that push this process harder in order to speed up amyloid-β removal.

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