Amyloid-β Fibrillogenesis Seeded by Interface-Induced Peptide Misfolding and Self-Assembly

The amphipathicity of the natively unstructured amyloid-β (Aβ40) peptide may play an important role in its aggregation into β-sheet rich fibrils, which is linked to the pathogenesis of Alzheimer's disease. Using the air/subphase interface as a model interface, we characterized Aβ's surface...

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Veröffentlicht in:	Biophysical journal 2010-05, Vol.98 (10), p.2299-2308
Hauptverfasser:	Chi, Eva Y., Frey, Shelli L., Winans, Amy, Lam, Kin Lok H., Kjaer, Kristian, Majewski, Jaroslaw, Lee, Ka Yee C.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amyloid - adverse effects Amyloid - chemistry Amyloid beta-Peptides - adverse effects Amyloid beta-Peptides - chemistry Amyloid beta-Protein Precursor Binding Sites Circular Dichroism - methods Lipid Bilayers - pharmacology Microscopy, Atomic Force - methods Peptide Fragments - pharmacology Peptides - adverse effects Peptides - pharmacology Protease Nexins Protein Protein Conformation Protein Folding - drug effects Proteostasis Deficiencies - etiology Receptors, Cell Surface Surface Properties
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