Nanoscale · 2012 · 196 citations · 24 references
Life SciencesBiochemistryBiophysicsMolecular BiophysicsStructural BiologyStructural BiophysicsAmyloid FormationBiomaterial CharacterizationFibrous ProteinsNanomechanical PropertiesProtein CharacterizationProtein StructureAmyloid FibrilsAmyloid StructureBovine Serum AlbuminFibril PolymorphismIntrinsic PropertiesMechanical Properties Of Protein MaterialsPeak Force MeasurementStructural Details
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.
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Structure of the cross-β spine of amyloid-like fibrils
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