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

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 homogen...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2002-12, Vol.124 (51), p.15150-15151
Main Authors: Lakdawala, Ami S, Morgan, David M, Liotta, Dennis C, Lynn, David G, Snyder, James P
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amyloid beta-Peptides - chemistry
Biological and medical sciences
Computer Simulation
Fundamental and applied biological sciences. Psychology
Hydrogen Bonding
Models, Molecular
Molecular and cellular biology
Molecular Sequence Data
Peptide Fragments - chemistry
Protein Structure, Secondary
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Summary: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.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja0273290