The molecular basis of interaction domains of fulllength PrP with lipid membranes

摘要

PrP-lipid membrane interactions are critical to PrP structural conversion and neurotoxicity, but its molecular mechanism remains unclear. A two-dimensional histogram of force-distance curves and a worm-like chain model revealed three binding regions at the PrP N-terminal, providing the molecular basis for understanding the interactions between full-length PrP and lipid membranes.