The Role of Structural Polymorphism in Driving the Mechanical Performance of the Alzheimer's Beta Amyloid Fibrils.

ABSTRACT: Alzheimer's Disease (AD) is related with the abnormal aggregation of amyloid β-peptides Aβ_1-40 and Aβ_1-42, the latter having a polymorphic character which gives rise to U- or S-shaped fibrils. Elucidating the role played by the nanoscale-material architecture on the amyloid fibril stability is a crucial breakthrough to better understand the pathological nature of amyloid structures and to support the rational design of bio-inspired materials. The computational study here presented highlights the superior mechanical behavior of the S-architecture, characterized by a Young's modulus markedly higher than the U-shaped architecture. The S-architecture showed a higher mechanical resistance to the enforced deformation along the fibril axis, consequence of a better interchain

SUBMITTER: Grasso G 

PROVIDER: S-EPMC6499180 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature