  Amyloid beta peptides (A\b{eta}), implicated in Alzheimers disease (AD),
interact with the cellular membrane and induce amyloid toxicity. The
composition of cellular membranes changes in aging and AD. We designed multi
component lipid models to mimic healthy and diseased states of the neuronal
membrane. Using atomic force microscopy (AFM), Kelvin probe force microscopy
(KPFM) and black lipid membrane (BLM) techniques, we demonstrated that these
model membranes differ in their nanoscale structure and physical properties,
and interact differently with A\b{eta}. Based on our data, we propose a new
hypothesis that changes in lipid membrane due to aging and AD may trigger
amyloid toxicity through electrostatic mechanisms, similar to the accepted
mechanism of antimicrobial peptide action. Understanding the role of the
membrane changes as a key activating amyloid toxicity may aid in the
development of a new avenue for the prevention and treatment of AD.
