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Structure and Mechanics of Amyloid Aggregates
Kilho Eom(엄길호),Hwan Young Woo(우환영),Bumjoon Choi(최범준),Sang Woo Lee(이상우) 대한기계학회 2015 대한기계학회 춘추학술대회 Vol.2015 No.11
Amyloid proteins, which are formed by the aggregation of proteins, have recently been highlighted due to not only their pathological roles but also their excellent mechanical properties such that the elastic modulus of amyloid aggregates is comparable to that of mechanically strong protein materials such as spider silk. For gaining insight into the fundamental mechanisms of amyloid formation as well as amyloid mechanics, we have studied what determines the structures and mechanical properties of amyloid aggregates with using all-atom molecular dynamics simulations and atomic force microscopy (AFM) experiments. From both all-atom molecular dynamics simulations and AFM imaging experiments, it is shown that the electrostatic interaction plays a crucial role in determining the structures of amyloid aggregates. We have also shown that the mechanical properties of amyloid aggregates are determined from their molecular structures such as steric zipper pattern, length scale, and structural hierarchy. Our work provides insight into the design principles showing how the excellent mechanical properties and structures of amyloid aggregates are determined, which will allow for developing novel biomimetic materials.
최범준(Bumjoon Choi),이상우(Sang Woo Lee),우환영(Hwan-Young Woo),엄길호(Kilho Eom) 대한기계학회 2014 대한기계학회 춘추학술대회 Vol.2014 No.11
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.