Dynamics and Fluidity of Amyloid Fibrils: A Model of Fibrous Protein Aggregates
- 28 November 2002
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 124 (51) , 15150-15151
- https://doi.org/10.1021/ja0273290
Abstract
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.Keywords
This publication has 5 references indexed in Scilit:
- Amyloid Structure: Models and Theoretical Considerations in Fibrous AggregatesJournal of the Chinese Chemical Society, 2002
- Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β-amyloid fibrilsProceedings of the National Academy of Sciences, 2000
- Dipolar recoupling NMR of biomolecular self-assemblies: determining inter- and intrastrand distances in fibrilized Alzheimer's β-amyloid peptideSolid State Nuclear Magnetic Resonance, 1998
- Cooperative Interaction between the Three Strands of a Designed Antiparallel β-SheetJournal of the American Chemical Society, 1998
- Structure of yeast triosephosphate isomerase at 1.9-.ANG. resolutionBiochemistry, 1990