Supramolecular Interactions and Morphology of Self-Assembling Peptide Amphiphile Nanostructures

M. Hussain Sangji, Hiroaki Sai, Stacey M. Chin, Sieun Ruth Lee, Ivan R Sasselli, Liam C. Palmer, Samuel I. Stupp*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

27 Scopus citations


The morphology of supramolecular peptide nanostructures is difficult to predict given their complex energy landscapes. We investigated peptide amphiphiles containing β-sheet forming domains that form twisted nanoribbons in water. We explained the morphology based on a balance between the energetically favorable packing of molecules in the center of the nanostructures, the unfavorable packing at the edges, and the deformations due to packing of twisted β-sheets. We find that morphological polydispersity of PA nanostructures is determined by peptide sequences, and the twisting of their internal β-sheets. We also observed a change in the supramolecular chirality of the nanostructures as the peptide sequence was modified, although only amino acids with l-configuration were used. Upon increasing charge repulsion between molecules, we observed a change in morphology to long cylinders and then rodlike fragments and spherical micelles. Understanding the self-assembly mechanisms of peptide amphiphiles into nanostructures should be useful to optimize their well-known functions.

Original languageEnglish (US)
Pages (from-to)6146-6155
Number of pages10
JournalNano letters
Issue number14
StatePublished - Jul 28 2021


  • nanostructure
  • peptide amphiphile
  • self-assembly
  • supramolecular chirality

ASJC Scopus subject areas

  • Condensed Matter Physics
  • Mechanical Engineering
  • Bioengineering
  • General Chemistry
  • General Materials Science


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