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

38Citations
Citations of this article
54Readers
Mendeley users who have this article in their library.

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 obtained a series of simple design rules that can be used to determine which polymorphs of a given sequence are most likely to form thermodynamically stable fibrils. These rules can potentially be employed to design peptide sequences that aggregate into a preferred polymorphic form for nanotechnological purposes. © 2011 by the Biophysical Society.

Cite

CITATION STYLE

APA

Berryman, J. T., Radford, S. E., & Harris, S. A. (2011). Systematic examination of polymorphism in amyloid fibrils by molecular-dynamics simulation. Biophysical Journal, 100(9), 2234–2242. https://doi.org/10.1016/j.bpj.2011.02.060

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free