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

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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@article{Lakdawala2002DynamicsAF, title={Dynamics and fluidity of amyloid fibrils: a model of fibrous protein aggregates.}, author={Ami S. Lakdawala and David M. Morgan and Dennis C Liotta and David G Lynn and James P. Snyder}, journal={Journal of the American Chemical Society}, year={2002}, volume={124 51}, pages={15150-1} }