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Updated: Jul 15, 2026

Visually Based Characterization of the Incipient Particle Motion in Regular Substrates: From Laminar to Turbulent Conditions
Published on: February 22, 2018
Dynamics and fluidity of amyloid fibrils: a model of fibrous protein aggregates
Ami S Lakdawala1, David M Morgan, Dennis C Liotta
1Center for the Analysis of Supramolecular Self-assemblies, Department of Chemistry, Department of Chemistry, Emory University, 1521 Pierce Drive, Atlanta, Georgia 30322, USA.
Abstract:
A previous experimentally defined model for the fibril formed from the core residues of the beta-amyloid (Abeta) peptides of Alzheimer's disease, 10YEVHHQKLVFFAEDVGSNKGAIIGLM, Abeta(10-35) using spectroscopic and scattering analyses reports on the average structure, benefiting immensely from the homogeneous assembly of Abeta(10-35). However, the energetic constraints that contribute to fibril dynamics and stability remain poorly understood. Here we perform molecular dynamics simulations to extend the structural assignment by providing evidence for a dynamic average ensemble with transient backbone H-bonds and internal solvation contributing to the inherent stability of amyloid fibrils.
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