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Self-assembly of minimal peptoid sequences

Castelletto, V., Seitsonen, J., Tewari, K. M., Hasan, A., Edkins, R. M., Ruokolainen, J., Pandey, L. M., Hamley, I. W. and Lau, K. H. A. (2020) Self-assembly of minimal peptoid sequences. ACS Macro Letters, 9 (4). pp. 494-499. ISSN 2161-1653

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To link to this item DOI: 10.1021/acsmacrolett.9b01010

Abstract/Summary

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.

Item Type:Article
Refereed:Yes
Divisions:Interdisciplinary centres and themes > Chemical Analysis Facility (CAF)
Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:90471
Publisher:American Chemical Society

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