Reversible Mechanical Unzipping of Amyloid β-Fibrils
作者： Miklós S. Z. Kellermayer , László Grama , Árpád Karsai , Attila Nagy , Amram Kahn
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摘要: Amyloid fibrils are self-associating filamentous structures, the deposition of which is considered to be one most important factors in pathogenesis Alzheimer's disease and various other disorders. Here we used single molecule manipulation methods explore mechanics structural dynamics amyloid fibrils. In mechanically manipulated fibrils, formed from either β (Aβ) peptides 1-40 or 25-35, β-sheets behave as elastic structures that can "unzipped" fibril with constant forces. The unzipping forces were different for Aβ1-40 Aβ25-35. Unzipping was fully reversible across a wide range stretch rates provided coupling, via β-sheet, between bound dissociated states maintained. rapid, cooperative zipping together could an mechanism behind self-assembly repetitive force patterns contribute mechanical fingerprint utilized characterization
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