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

Overview

Journal Front Bioeng Biotechnol

Date 2019 May 21

PMID 31106199

Citations 7

Authors

Gianvito Grasso

Martina Rebella

Umberto Morbiducci

Jack A Tuszynski

Andrea Danani

Marco A Deriu

Affiliations

Soon will be listed here.

Abstract

Alzheimer's Disease (AD) is related with the abnormal aggregation of amyloid β-peptides Aβ and Aβ, 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 hydrogen bonds' distribution. In conclusion, this study, focusing the attention on the pivotal multiscale relationship between molecular phenomena and material properties, suggests the S-shaped Aβ species as a target of election in computational screen/design/optimization of effective aggregation modulators.

Citing Articles

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