Liquid and Hydrogel Phases of PrP Linked to Conformation Shifts and Triggered by Alzheimer's Amyloid-β Oligomers.

Protein phase separation by low-complexity, intrinsically disordered domains generates membraneless organelles and links to neurodegeneration. Cellular prion protein (PrP) contains such domains, causes spongiform degeneration, and is a receptor for Alzheimer's amyloid-β oligomers (Aβo). Here, we show that PrP separates as a liquid phase, in which α-helical Thr become unfolded.