Poly-unsaturated omega-3 fatty acids are increasingly proposed as dietary supplements able to reduce the risk of development or progression of the Alzheimer's disease (AD). To date, the molecular mechanism through which these lipids act has not been yet univocally identified. In this work, we investigate whether omega-3 fatty acids could interfere with the fate of the Alzheimer-related amyloid peptide by tuning the microstructural and dynamical properties of the neuronal membrane. To this aim, the influence of the omega-3 lipid 1,2-didocosahexaenoyl-sn-glycero-3-phosphocholine (22:6(cis)PC) on the biophysical properties of lipid bilayers and on their interaction with the amyloid peptide fragment Aβ(25-35) has been investigated by Electron Spin resonance (ESR), using spin-labeled phospholipids. The results show that the peptide selectively interacts with bilayers enriched in cholesterol (Chol) and sphingomyelin (SM). (22:6(cis)PC) enhances the Aβ(25-35)/membrane interaction, favouring a deeper internalization of the peptide among the lipid acyl chains, and consequently hindering its pathogenic self-aggregation.

Omega-3 Fatty Acids Regulate the Interaction of the Alzheimer’s Aβ(25–35) Peptide with Lipid Membranes

D'URSI, Anna Maria;
2013

Abstract

Poly-unsaturated omega-3 fatty acids are increasingly proposed as dietary supplements able to reduce the risk of development or progression of the Alzheimer's disease (AD). To date, the molecular mechanism through which these lipids act has not been yet univocally identified. In this work, we investigate whether omega-3 fatty acids could interfere with the fate of the Alzheimer-related amyloid peptide by tuning the microstructural and dynamical properties of the neuronal membrane. To this aim, the influence of the omega-3 lipid 1,2-didocosahexaenoyl-sn-glycero-3-phosphocholine (22:6(cis)PC) on the biophysical properties of lipid bilayers and on their interaction with the amyloid peptide fragment Aβ(25-35) has been investigated by Electron Spin resonance (ESR), using spin-labeled phospholipids. The results show that the peptide selectively interacts with bilayers enriched in cholesterol (Chol) and sphingomyelin (SM). (22:6(cis)PC) enhances the Aβ(25-35)/membrane interaction, favouring a deeper internalization of the peptide among the lipid acyl chains, and consequently hindering its pathogenic self-aggregation.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11386/4113053
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