Omega-3 fatty acids regulate the interaction of the Alzheimer's aβ(25-35) peptide with lipid membranes

Polyunsaturated 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 in...

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Veröffentlicht in:Langmuir : the ACS journal of surfaces and colloids. - 1985. - 29(2013), 46 vom: 19. Nov., Seite 14239-45
1. Verfasser: Vitiello, Giuseppe (VerfasserIn)
Weitere Verfasser: Di Marino, Sara, D'Ursi, Anna Maria, D'Errico, Gerardino
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2013
Zugriff auf das übergeordnete Werk:Langmuir : the ACS journal of surfaces and colloids
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Amyloid beta-Peptides Fatty Acids, Omega-3 Lipid Bilayers Peptide Fragments Phospholipids Spin Labels amyloid beta-protein (25-35)
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520 |a Polyunsaturated 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, favoring a deeper internalization of the peptide among the lipid acyl chains and, consequently, hindering its pathogenic self-aggregation 
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650 4 |a Research Support, Non-U.S. Gov't 
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650 7 |a Fatty Acids, Omega-3  |2 NLM 
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650 7 |a Peptide Fragments  |2 NLM 
650 7 |a Phospholipids  |2 NLM 
650 7 |a Spin Labels  |2 NLM 
650 7 |a amyloid beta-protein (25-35)  |2 NLM 
700 1 |a Di Marino, Sara  |e verfasserin  |4 aut 
700 1 |a D'Ursi, Anna Maria  |e verfasserin  |4 aut 
700 1 |a D'Errico, Gerardino  |e verfasserin  |4 aut 
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