Molecular dynamics simulation of β-sheet formation in self-assembled peptide amphiphile fibers

One Sun Lee, Yamei Liu, George C. Schatz*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

24 Scopus citations


The influence of amino acid sequence on the secondary structure of peptide amphiphile (PAs) cylindrical micelles and fibers that are self-assembled in solution is studied using molecular dynamics simulations. Simulations for two choices of PAs were performed, starting with structures that have the correct overall shape, but which restructure considerably during the simulation, with one fiber being composed of valine rich PAs and the other of alanine rich PAs. Self-assembly is similar in both simulations, with stable fibers (diameter is 7.7-8 nm) obtained after 40 ns. We find that the valine rich PA fiber has a higher β-sheet population than the alanine rich fiber, and that the number of hydrogen bonds is higher. This behavior of the valine rich fiber is consistent with experimental measurements of higher stiffness, and it shows that stiffness can be varied while still maintaining self-assembly.

Original languageEnglish (US)
Article number936
JournalJournal of Nanoparticle Research
Issue number8
StatePublished - Aug 2012


  • Clusters
  • Modeling and simulation
  • Molecular dynamics simulation
  • Peptide amphiphiles
  • Secondary structure
  • Storage modulus
  • β-Sheet

ASJC Scopus subject areas

  • Bioengineering
  • Chemistry(all)
  • Atomic and Molecular Physics, and Optics
  • Modeling and Simulation
  • Materials Science(all)
  • Condensed Matter Physics


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