Dynamics and Fluidity of Amyloid Fibrils:  A Model of Fibrous Protein Aggregates

Ami S. Lakdawala,† David M. Morgan,‡ Dennis C. Liotta,† David G. Lynn,*‡ and James P. Snyder*†
Center for the Analysis of Supramolecular Self-assemblies, Department of Chemistry, Departments of Chemistry and Biology, Emory University, 1521 Pierce Drive, Atlanta, Georgia 30322
J. Am. Chem. Soc., 2002, 124 (51), pp 15150–15151
DOI: 10.1021/ja0273290
Publication Date (Web): November 28, 2002
Copyright © 2002 American Chemical Society
†

 Department of Chemistry.

,
‡

 Departments of Chemistry and Biology.

,
*

 Authors for correspondence. E-mail:  snyder@euch4e.chem.emory.edu; dlynn2@emory.edu.

Abstract

Abstract Image

A previous experimentally defined model for the fibril formed from the core residues of the β-amyloid (Aβ) peptides of Alzheimer's disease, 10YEVHHQKLVFFAEDVGSNKGAIIGLM, Aβ(10−35) using spectroscopic and scattering analyses reports on the average structure, benefiting immensely from the homogeneous assembly of Aβ(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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History

  • Published In Issue December 25, 2002
  • Received June 17, 2002

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