Amyloid fibrils, which play a vital role on disease expression, have recently been found to exhibit the excellent mechanical properties such as elastic modulus in the order of 10 GPa, which is comparable to mechanically strong proteins such as spider ...
Amyloid fibrils, which play a vital role on disease expression, have recently been found to exhibit the excellent mechanical properties such as elastic modulus in the order of 10 GPa, which is comparable to mechanically strong proteins such as spider silk protein. We study the mechanical deformation mechanisms and properties of amyloid fibrils by using atomistic simulations. It is shown that the legnth scale of amyloid fibril governs its deformation mechanisms in such a way that shear deformation dominates the mechanics of a short amyloid fibril with its length of 10 nm. The length-dependent bending behavior of amyloid fibrils has been well depicted by Timoshenko beam model. Our study highlights the mechanical deformation mechanisms and properties of protein fibrils are governed by their structural features such as length scales.