Self-assembly of minimal peptoid sequences

Valeria Castelletto, Jani Seitsonen, Kunal M. Tewari, Abshar Hasan, Robert M. Edkins, Janne Ruokolainen, Lalit M. Pandey, Ian W. Hamley, King Hang Aaron Lau

Research output: Contribution to journalLetterpeer-review

8 Citations (Scopus)
8 Downloads (Pure)

Abstract

Peptoids are biofunctional N-substituted glycine peptidomimics. Their self-assembly is of fundamental interest because they demonstrate alternatives to conventional peptide structures based on backbone chirality and beta-sheet hydrogen bonding. The search for self-assembling, water-soluble "minimal" sequences, be they peptide or peptidomimic, is a further challenge. Such sequences are highly desired for their compatibility with biomacromolecules and convenient synthesis for broader application. We report the self-assembly of a set of trimeric, water-soluble α-peptoids that exhibit a relatively low critical aggregation concentration (CAC ∼0.3 wt %). Cryo-EM and angle-resolved DLS show different sequence-dependent morphologies, namely uniform ca. 6 nm wide nanofibers, sheets, and clusters of globular assemblies. Absorbance and fluorescence spectroscopies indicate unique phenyl environments for π-interactions in the highly ordered nanofibers. Assembly of our peptoids takes place when the sequences are fully ionized, representing a departure from superficially similar amyloid-type hydrogen-bonded peptide nanostructures and expanding the horizons of assembly for sequence-specific bio- and biomimetic macromolecules.

Original languageEnglish
Pages (from-to)494-499
Number of pages6
JournalACS Macro Letters
Volume9
Issue number4
Early online date19 Mar 2020
DOIs
Publication statusPublished - 21 Apr 2020

Keywords

  • self-assembly
  • nanostructure
  • biomacromolecules
  • peptoids
  • peptide mimics
  • dynamic light scattering
  • cryo-EM
  • pi stacking
  • hydrogen bonding

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