ArticleBeilstein journal of nanotechnology2013
Molecular dynamics simulations of mechanical failure in polymorphic arrangements of amyloid fibrils containing structural defects.
Article in Beilstein journal of nanotechnology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Roles of Tryptophan and Charged Residues on the Polymorphisms of Amyloids Formed by K-Peptides of Hen Egg White Lysozyme Investigated through Molecular Dynamics Simulations.International journal of molecular sciences · 2023Article
- Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis.Nature communications · 2021Article
- Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs.Chemical Society reviews · 2014Review
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We examine how the different steric packing arrangements found in amyloid fibril polymorphs can modulate their mechanical properties using steered molecular dynamics simulations. Our calculations demonstrate that for fibrils containing structural defects, their ability to resist force in a particular direction can be dominated by both the number and molecular details of the defects that are present. The simulations thereby suggest a hierarchy of factors that govern the mechanical resilience of fibrils, and illustrate the general principles that must be considered when quantifying the mechanical properties of amyloid fibres containing defects.
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