Imaging Amyloid-β Membrane Interactions; Ion-channel pores and Lipid-Bilayer Permeability in Alzheimer's Disease.
TL;DR: Aβ self-associates into a series of complex assemblies with different structural and biophysical properties, which results in membrane permeability and loss of cellular homeostasis as discussed by the authors .
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Abstract: The accumulation of the amyloid-β peptides (Aβ) is central to the development of Alzheimer's disease. The mechanism by which Aβ triggers a cascade of events that leads to dementia is a topic of intense investigation. Aβ self-associates into a series of complex assemblies with different structural and biophysical properties. It is the interaction of these oligomeric, protofibril and fibrillar assemblies with lipid membranes, or with membrane receptors, that results in membrane permeability and loss of cellular homeostasis, a key event in Alzheimer's disease pathology. Aβ can have an array of impacts on lipid membranes, reports have included: a carpeting effect; a detergent effect; and Aβ ion-channel pore formation. Recent advances imaging these interactions are providing a clearer picture of Aβ induced membrane disruption. Understanding the relationship between different Aβ structures and membrane permeability will inform therapeutics targeting Aβ cytotoxicity.
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Imaging Amyloid-β Membrane Interactions; Ion-channel pores and Lipid-Bilayer Permeability in Alzheimer's Disease.
TL;DR: Aβ self-associates into a series of complex assemblies with different structural and biophysical properties, which results in membrane permeability and loss of cellular homeostasis as discussed by the authors .
29
Mechanosensitive Piezo1 channel in physiology and pathophysiology of the central nervous system
Bo Zong,Feng-Yuan Yu,Xiaoyun Zhang,Yige Pang,Wenrui Zhao,Peng Sun,Lin Li +6 more
TL;DR: The review discusses the current understanding of the involvement of the Piezo1 channel in central nervous system disorders, such as Alzheimer's disease, multiple sclerosis, glaucoma, stroke, and glioma.
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Cholesterol and Lipid Rafts in the Biogenesis of Amyloid-β Protein and Alzheimer's Disease.
George A. Pantelopulos,Conor B. Abraham,John E Straub +2 more
TL;DR: This work proposes that cholesterol impacts the genesis of Aβ not through direct interaction with proteins in the bilayer, but indirectly by inducing the liquid-ordered phase and accompanying liquid-liquid phase separations, which partition proteins in the amyloid cascade to different lipid domains and ultimately to different endocytotic pathways.
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The Role of Amyloid β-Biomembrane Interactions in the Pathogenesis of Alzheimer's Disease: Insights from Liposomes as Membrane Models.
TL;DR: A recent review as discussed by the authors summarizes the latest findings on this field using liposomes as biomembrane model, as they are considered the most promising 3D model, and the current challenges and future directions are discussed.
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Cu2+-induced modification of the kinetics of Aβ(1-42) channels
Randa Bahadi,Peter V. Farrelly,Bronwyn L. Kenna,Cyril C. Curtain,Colin L. Masters,Roberto Cappai,Kevin J. Barnham,Joseph I. Kourie +7 more
TL;DR: It is found that the amyloid β peptide Aβ(1-42) is capable of interacting with membrane and forming heterogeneous ion channels in the absence of any added Cu2+ or biological redox agents.
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Membrane-Catalyzed Aggregation of Islet Amyloid Polypeptide Is Dominated by Secondary Nucleation
TL;DR: In this article , the authors use kinetic analysis to elucidate the aggregation mechanism of IAPP in the presence of mixed zwitterionic and anionic lipid membranes, and they converge to a model in which aggregation on the membrane is strongly dominated by secondary nucleation, that is, the formation of new nuclei on the surface of existing fibrils.
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Cholesterol Modulates the Formation of the Aβ Ion Channel in Lipid Bilayers.
TL;DR: A possible approach to consider cholesterol levels for the treatment of AD patients is suggested, as a small amount of cholesterol interacted with Aβ and facilitated Aβ ion-channel formation in the membrane.
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Therapeutic potential for amyloid surface inhibitor: only amyloid‐β oligomers formed by secondary nucleation disrupt lipid membrane integrity
TL;DR: This study highlights the therapeutic potential for inhibiting secondary nucleation process in Aβ aggregation, rather than inhibiting all pathways to fibril formation, by incubating Aβ monomers with cHASI and showing that only oligomers produced during secondary surface nucleation disrupt membrane integrity.
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