Dynamics and fluidity of amyloid fibrils: a model of fibrous protein aggregates

Ami S Lakdawala, David M Morgan, Dennis C Liotta, David G Lynn, James P Snyder
Journal of the American Chemical Society 2002 December 25, 124 (51): 15150-1
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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