Abstract
We report the investigation of the mechanical properties of different types of amyloid fibrils by the peak force quantitative nanomechanical (PF-QNM) technique. We demonstrate that this technique correctly measures the Young's modulus independent of the polymorphic state and the cross-sectional structural details of the fibrils, and we show that values for amyloid fibrils assembled from heptapeptides, α-synuclein, Aβ(1-42), insulin, β-lactoglobulin, lysozyme, ovalbumin, Tau protein and bovine serum albumin all fall in the range of 2-4 GPa.
MeSH terms
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Amyloid / chemistry*
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Amyloid / metabolism
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Amyloid beta-Peptides / chemistry
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Amyloid beta-Peptides / metabolism
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Animals
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Cattle
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Elastic Modulus
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Lactoglobulins / chemistry
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Lactoglobulins / metabolism
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Muramidase / chemistry
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Muramidase / metabolism
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Nanotechnology / methods*
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Ovalbumin / chemistry
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Ovalbumin / metabolism
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Peptide Fragments / chemistry
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Peptide Fragments / metabolism
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Serum Albumin, Bovine / chemistry
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Serum Albumin, Bovine / metabolism
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alpha-Synuclein / chemistry
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alpha-Synuclein / metabolism
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tau Proteins / chemistry
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tau Proteins / metabolism
Substances
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Amyloid
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Amyloid beta-Peptides
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Lactoglobulins
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Peptide Fragments
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alpha-Synuclein
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amyloid beta-protein (1-42)
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tau Proteins
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Serum Albumin, Bovine
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Ovalbumin
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Muramidase