Stabilization of a Membrane-Associated Amyloid-β Oligomer for Its Validation in Alzheimer's Disease.

ABSTRACT: We have recently reported on the preparation of a membrane-associated β-barrel Pore-Forming Aβ42 Oligomer (βPFOAβ42). It corresponds to a stable and homogeneous Aβ42 oligomer that inserts into lipid bilayers as a well-defined pore and adopts a specific structure with characteristics of a β-barrel arrangement. As a follow-up of this work, we aim to establish βPFOAβ42's relevance in Alzheimer's disease (AD). However, βPFOAβ42 is formed under dodecyl phosphocholine (DPC) micelle conditions-intended to mimic the hydrophobic environment of membranes-which are dynamic. Consequently, dilution of the βPFOAβ42/DPC complex in a detergent-free buffer leads to dispersion of the DPC molecules from the oligomer surface, leaving the oligomer without the hydrophobic micelle belt that stabilizes it. Since

SUBMITTER: Serra-Batiste M 

PROVIDER: S-EPMC5917194 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature