Systematic examination of polymorphism in amyloid fibrils by molecular-dynamics simulation.

ABSTRACT: Amyloid fibrils often exhibit polymorphism. Polymorphs are formed when proteins or peptides with identical sequences self-assemble into fibrils containing substantially different arrangements of the β-strands. We used atomistic molecular-dynamics simulation to examine the thermodynamic stability of a amyloid fibrils in different polymorphic forms by performing a systematic investigation of sequence and symmetry space for a series of peptides with a range of physicochemical properties. We show that the stability of fibrils depends on both sequence and the symmetry because these factors determine the availability of favorable interactions between the peptide strands within a sheet and in intersheet packing. By performing a detailed analysis of these interactions as a function of symmetry, we

SUBMITTER: Berryman JT 

PROVIDER: S-EPMC3149254 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature