Self-Assembly of Minimal Peptoid Sequences

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A1 Alkuperäisartikkeli tieteellisessä aikakauslehdessä

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en

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6

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ACS Macro Letters, Volume 9, issue 4, pp. 494-499

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 ?-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.

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Castelletto, V, Seitsonen, J, Tewari, K M, Hasan, A, Edkins, R M, Ruokolainen, J, Pandey, L M, Hamley, I W & Lau, K H A 2020, 'Self-Assembly of Minimal Peptoid Sequences', ACS Macro Letters, vol. 9, no. 4, pp. 494-499. https://doi.org/10.1021/acsmacrolett.9b01010