Abstract
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-β 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- peptide, and the peptide fragment amyloid- 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.
Highlights
Alzheimer’s disease is a degenerative brain illness, characterized by progressive deterioration of the brain
The membranes are well oriented in lamellar structures allowing for information in and out of the lipid membrane plane to be collected simultaneously
The location of the (1–42) residue full-length peptide in Figures 7b and d was modeled with the hydrophilic part of the peptide occupying a position on the surface of the bilayer, and the hydrophobic part of the peptide residing in the membrane core, parallel to the lipid tails
Summary
Alzheimer’s disease is a degenerative brain illness, characterized by progressive deterioration of the brain. The first explanations placed the origin of the symptoms on “senile plaques”, proteinous deposits in the extracellular regions of the brain containing fibrillar amyloid-β (Aβ) peptides [1] This hypothesis has been pursued, in recent years, a new hypothesis has emerged, placing toxicity on membrane active monomers and oligomers of Aβ [2,3,4,5,6]. Membranes to observe the equilibrium structure of an anionic lipid bilayer containing cholesterol and amyloid-β peptides. Membranes containing a high, physiologically relevant, amount of cholesterol with amyloid-β peptides were created This allowed us to study the interaction of the full-length (1–42) and the (22–40) fragment amyloid-β peptide in cholesterol rich anionic membranes
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