Asymmetric Peptide Nanoribbons

Zhilin Yu, Faifan Tantakitti, Liam C. Palmer, Samuel I Stupp

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Asymmetry in chemical structure or shape at molecular, nanoscale, or microscopic levels is essential to a vast number of functionalities in both natural and artificial systems. Bottom-up approaches to create asymmetric supramolecular nanostructures are considered promising but this strategy suffers from the potentially dynamic nature of noncovalent interactions. We report here on supramolecular self-assembly of asymmetric peptide amphiphiles consisting of two different molecularly linked domains. We found that strong noncovalent interactions and a high degree of internal order among the asymmetric amphiphiles lead to nanoribbons with asymmetric faces due to the preferential self-association of the two domains. The capture of gold nanoparticles on only one face of the nanoribbons demonstrates symmetry breaking in these supramolecular structures.

Original languageEnglish
Pages (from-to)6967-6974
Number of pages8
JournalNano Letters
Volume16
Issue number11
DOIs
Publication statusPublished - Nov 9 2016

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Keywords

  • Asymmetric nanostructures
  • multidomain peptide amphiphiles
  • nanoribbons
  • supramolecular self-assembly

ASJC Scopus subject areas

  • Bioengineering
  • Chemistry(all)
  • Materials Science(all)
  • Condensed Matter Physics
  • Mechanical Engineering

Cite this

Yu, Z., Tantakitti, F., Palmer, L. C., & Stupp, S. I. (2016). Asymmetric Peptide Nanoribbons. Nano Letters, 16(11), 6967-6974. https://doi.org/10.1021/acs.nanolett.6b03062