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• W2225101735 abstract "Amyloid fibrils have recently been considered as an interesting material, since they exhibit the excellent mechanical properties such as elastic modulus in the order of 10 GPa, which is larger than that of other protein materials. Despite recent findings of these excellent mechanical properties for amyloid fibrils, it has not been fully understood how these excellent mechanical properties are achieved. In this work, we have studied the nanomechanical deformation behaviors and properties of amyloid fibrils such as their elastic modulus as well as fracture strength, by using atomistic simulations, particularly steered molecular dynamics simulations. Our simulation results suggest the important role of the length of amyloid fibrils in their mechanical properties such that the fracture force of amyloid fibril is increased when the fibril length decreases. This length scale effect is attributed to the rupture mechanisms of hydrogen bonds that sustain the fibril structure. Moreover, we have investigated the effect of boundary condition on the nanomechanical deformation mechanisms of amyloid fibrils. It is found that the fracture force is critically affected by boundary condition. Our study highlights the crucial role of both fibril length and boundary condition in the nanomechanical properties of amyloid fibrils." @default.
• W2225101735 created "2016-06-24" @default.
• W2225101735 creator A5004450273 @default.
• W2225101735 creator A5008010244 @default.
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• W2225101735 date "2016-01-25" @default.
• W2225101735 modified "2023-10-15" @default.
• W2225101735 title "Nanomechanical behaviors and properties of amyloid fibrils" @default.
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• W2225101735 doi "https://doi.org/10.12989/mmm.2016.1.1.053" @default.
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