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

Langmuir. 2011 May 17;27(10):6163-70. doi: 10.1021/la200800e. Epub 2011 Apr 13.


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 α 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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Hydrophobic and Hydrophilic Interactions*
  • Magnesium / pharmacology
  • Molecular Imaging
  • Molecular Sequence Data
  • Peptides / chemistry*
  • Peptides / metabolism*
  • Protein Binding / drug effects
  • Protein Folding / drug effects
  • Protein Structure, Secondary
  • Solutions


  • Peptides
  • Solutions
  • Magnesium