Effect of the peptide secondary structure on the peptide amphiphile supramolecular structure and interactions

Dimitris Missirlis, Arkadiusz Chworos, Caroline J. Fu, Htet A. Khant, Daniel V. Krogstad, Matthew Tirrell

Research output: Contribution to journalArticle

Abstract

Bottom-up fabrication of self-assembled nanomaterials requires control over forces and interactions between building blocks. We report here on the formation and architecture of supramolecular structures constructed from two different peptide amphiphiles. Inclusion of four alanines between a 16-mer peptide and a 16 carbon long aliphatic tail resulted in a secondary structure shift of the peptide headgroups from R helices to β sheets. A concomitant shift in self-assembled morphology from nanoribbons to core-shell worm-like micelles was observed by cryogenic transmission electron microscopy (cryo-TEM) and atomic force microscopy (AFM). In the presence of divalent magnesium ions, these a priori formed supramolecular structures interacted in distinct manners, highlighting the importance of peptide amphiphile design in self-assembly.

Original languageEnglish (US)
Pages (from-to)6163-6170
Number of pages8
JournalLangmuir
Volume27
Issue number10
DOIs
StatePublished - Jun 1 2011
Externally publishedYes

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ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Spectroscopy
  • Electrochemistry

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