Quantitative Analysis of the Influence of Trehalose on Amyloid-β Binding to Membranes by Localized Surface Plasmon Resonance Spectroscopy.

The damaging effect of amyloid-β (Aβ) on cellular membranes is an essential factor that contributes to Aβ's neurotoxicity in Alzheimer's disease. In this work, we explore the role of trehalose sugar in protecting model lipid membranes composed of DPPC-POPC-Cholesterol against Aβ toxicity. We used localized surface plasmon resonance (LSPR) spectroscopy and conducted a quantitative analysis to study the influence of trehalose on Aβ-membrane interactions. The LSPR data indicate that trehalose can effectively reduce the level of binding of Aβ to the lipid membrane, indicating its protective role against amyloid toxicity. Additionally, atomic force microscopy (AFM) was used to visualize the lipid membranes supported on the LSPR sensors and to elucidate the effect of trehalose on membrane morphology. The ability of trehalose to alter the physical properties of model membranes is discussed in relation to its protective role against Aβ during dehydration.