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

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

8 Citations (Scopus)
70 Downloads (Pure)


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 ?-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
Issue number4
Publication statusPublished - 21 Apr 2020
MoE publication typeA1 Journal article-refereed

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