Molecular simulation study of peptide amphiphile self-assembly

Yuri S. Velichko, Samuel I. Stupp, Monica Olvera De La Cruz*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

184 Scopus citations


We study the self-assembly of peptide amphiphile (PA) molecules, which is governed by hydrophobic interactions between alkyl tails and a network of hydrogen bonds between peptide blocks. We demonstrate that the interplay between these two interactions results in the formation of assemblies of different morphology, in particular, single β-sheets connected laterally by hydrogen bonds, stacks of parallel β-sheets, spherical micelles, micelles with β-sheets in the corona, and long cylindrical fibers. We characterize the size distribution of the aggregates as a function of the molecular interactions. Our results suggest that the formation of nanofibers of peptide amphiphiles obeys an open association model, which resembles living polymerization.

Original languageEnglish (US)
Pages (from-to)2326-2334
Number of pages9
JournalJournal of Physical Chemistry B
Issue number8
StatePublished - Feb 28 2008

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry


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