Journal
FRONTIERS IN BIOENGINEERING AND BIOTECHNOLOGY
Volume 7, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fbioe.2019.00083
Keywords
biomechanics; amyloid fibrils; molecular dynamics simulations; Alzheimer's Disease; Young Modulus; structural polymorphism
Funding
- Swiss National Supercomputing Centre (CSCS)
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Alzheimer's Disease (AD) is related with the abnormal aggregation of amyloid beta-peptides A beta(1-40) and A beta(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 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 A beta(1-42) species as a target of election in computational screen/design/optimization of effective aggregation modulators.
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