ArticleACS omega2025
Quantitative Analysis of the Influence of Trehalose on Amyloid-β Binding to Membranes by Localized Surface Plasmon Resonance Spectroscopy.
Article in ACS omega, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Trehalose's untapped mechanisms in alzheimer's: gut-brain-autophagy signalling beyond the usual targets.Daru : journal of Faculty of Pharmacy, Tehran University of Medical Sciences · 2026Review
- Amyloid β 1-42 Can Form Ion Channels as Small as Gramicidin in Model Lipid Membranes.Membranes · 2025Article
Corrections and comments
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Authors and funding
3 authors.
Funding
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Abstract
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.
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Registered trials
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