Interaction of full-length Tau with negatively charged lipid membranes leads to polymorphic aggregates
Vicky Ury‐Thiery, Yann Fichou, Isabel D. Alves, Michaël Molinari, Sophie Lecomte, Cécile Feuillie
Abstract
in the micromolar range, indicating the deposition of a thick protein layer. Atomic force microscopy (AFM) real-time imaging allows the observation of partial lipid solubilization and the deposition of polymorphic aggregates in the form of thick patches and fibrillary structures resembling amyloid fibers, which could grow from a combination of extracted anionic phospholipids from the membrane and Tau protein. This study deepens our understanding of full-length Tau's multifaceted interactions with lipids, shedding light on potential mechanisms leading to the formation of pathogenic Tau assemblies.
Topics & Concepts
MembraneLipid bilayerChemistryBiophysicsMaterials scienceBiochemistryBiologyLipid Membrane Structure and BehaviorProtein Structure and DynamicsNeuroscience and Neuropharmacology Research