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 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.
Lakdawala
Ami S
AS
Center for the Analysis of Supramolecular Self-assemblies, Department of Chemistry, Department of Chemistry, Emory University, 1521 Pierce Drive, Atlanta, Georgia 30322, USA.
Morgan
David M
DM
Liotta
Dennis C
DC
Lynn
David G
DG
Snyder
James P
JP
D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000737:chemistry*; D003198:Computer Simulation; D006860:Hydrogen Bonding; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments; C407125:amyloid beta-protein (10-35)