Multiscale and Multiphysics Mechanics

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Nanomechanical behaviors and properties of amyloid fibrils

  • Choi, Bumjoon (Department of Biomedical Engineering, Yonsei University) ;
  • Lee, Sang Woo (Department of Biomedical Engineering, Yonsei University) ;
  • Eom, Kilho (Biomechanics Laboratory, College of Sport Science, Sungkyunkwan University)
  • Received : 2015.04.03
  • Accepted : 2015.10.22
  • Published : 2016.01.25
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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.

Keywords

Acknowledgement

Supported by : National Research Foundation of Korea (NRF), Korea Institute of Science and Technology Information (KISTI)

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