Molecular dynamics study of structural properties of β-sheet assemblies formed by synthetic de novo oligopeptides

We study, by means of molecular dynamics (MD) simulations with explicit water, the structure and stability of β-sheet tapes, ribbons and double ribbons formed by rationally designed oligopeptides P11-I and P11-II in aqueous solutions. Two different methods for the treatment of the electrostatic interactions were considered: a smoothly shifted spherical cutoff approach under spherical harmonic conditions, and the particle mesh Ewald technique. We investigate the transfer of chirality from single L-aminoacids to the molecular scale of oligopeptides and from the latter to the supramolecular scale of peptide clusters. Furthermore, we obtain structural data for the representative conformations of these clusters, as well as study various average properties of their geometry.