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Open AccessArticle

The Position of Aβ22-40 and Aβ1-42 in Anionic Lipid Membranes Containing Cholesterol

Soft Matter and Functional Materials, Helmholtz-Zentrum Berlin für Materialien und Energie, Lise-Meitner-Campus, Berlin, Germany
Department of Physics and Astronomy, McMaster University, Hamilton, ON L8S 4M1, Canada
Author to whom correspondence should be addressed.
Academic Editor: Shiro Suetsugu
Membranes 2015, 5(4), 824-843;
Received: 30 September 2015 / Accepted: 25 November 2015 / Published: 30 November 2015
(This article belongs to the Special Issue Membrane Structure and Dynamics)
Amyloid-β peptides interact with cell membranes in the human brain and are associated with neurodegenerative diseases, such as Alzheimer’s disease. An emerging explanation of the molecular mechanism, which results in neurodegeneration, places the cause of neurotoxicity of the amyloid- peptides on their potentially negative interaction with neuronal membranes. It is known that amyloid-β peptides interact with the membrane, modifying the membrane’s structural and dynamic properties. We present a series of X-ray diffraction experiments on anionic model lipid membranes containing various amounts of cholesterol. These experiments provide experimental evidence for an interaction of both the full length amyloid-β1-42 peptide, and the peptide fragment amyloid-β22-40 with anionic bilayer containing cholesterol. The location of the amyloid-β peptides was determined from these experiments, with the full length peptide embedding into the membrane, and the peptide fragment occupying 2 positions—on the membrane surface and embedded into the membrane core. View Full-Text
Keywords: lipid membranes; cholesterol; Alzheimer’s disease; amyloid-β; X-ray diffraction lipid membranes; cholesterol; Alzheimer’s disease; amyloid-β; X-ray diffraction
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Barrett, M.A.; Alsop, R.J.; Hauß, T.; Rheinstädter, M.C. The Position of Aβ22-40 and Aβ1-42 in Anionic Lipid Membranes Containing Cholesterol. Membranes 2015, 5, 824-843.

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