A coarse-grained molecular dynamics investigation on spontaneous binding of Aβ_1-40 fibrils with cholesterol-mixed DPPC bilayers.

ABSTRACT: Alzheimer's disease is the most common form of dementia. Its aetiology is characterized by the misfolding and aggregation of amyloid-β (Aβ) peptides into β-sheet-rich Aβ oligomers/fibrils. Although multiple experimental studies have suggested that Aβ oligomers/fibrils interact with the cell membranes and perturb their structures and dynamics, the molecular mechanism of this interaction is still not fully understood. In the present work, we have performed a total of 120 μs-long simulations to investigate the interaction between trimeric or hexameric Aβ_1-40 fibrils with either a 100% DPPC bilayer, a 70% DPPC-30% cholesterol bilayer or a 50% DPPC-50% cholesterol bilayer. Our simulation data capture the spontaneous binding of the aqueous Aβ_1-40 fibrils with the membranes

SUBMITTER: Agrawal N 

PROVIDER: S-EPMC10151222 | biostudies-literature | 2023

REPOSITORIES: biostudies-literature