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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.