Molecular simulation study of peptide amphiphile self-assembly

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

Research output: Contribution to journalArticle

148 Citations (Scopus)

Abstract

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
Pages (from-to)2326-2334
Number of pages9
JournalJournal of Physical Chemistry B
Volume112
Issue number8
DOIs
Publication statusPublished - Feb 28 2008

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Amphiphiles
Self assembly
Peptides
peptides
self assembly
Micelles
micelles
Hydrogen bonds
hydrogen bonds
Living polymerization
Molecular interactions
simulation
molecular interactions
Nanofibers
assemblies
coronas
polymerization
Association reactions
interactions
Molecules

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry

Cite this

Molecular simulation study of peptide amphiphile self-assembly. / Velichko, Yuri S.; Stupp, Samuel I; De La Cruz, Monica Olvera.

In: Journal of Physical Chemistry B, Vol. 112, No. 8, 28.02.2008, p. 2326-2334.

Research output: Contribution to journalArticle

Velichko, Yuri S. ; Stupp, Samuel I ; De La Cruz, Monica Olvera. / Molecular simulation study of peptide amphiphile self-assembly. In: Journal of Physical Chemistry B. 2008 ; Vol. 112, No. 8. pp. 2326-2334.
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