TY - JOUR
T1 - Self-Assembly of Minimal Peptoid Sequences
AU - Castelletto, Valeria
AU - Seitsonen, Jani
AU - Tewari, Kunal M.
AU - Hasan, Abshar
AU - Edkins, Robert M.
AU - Ruokolainen, Janne
AU - Pandey, Lalit M.
AU - Hamley, Ian W.
AU - Lau, King Hang Aaron
PY - 2020/4/21
Y1 - 2020/4/21
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85082419654&partnerID=8YFLogxK
U2 - 10.1021/acsmacrolett.9b01010
DO - 10.1021/acsmacrolett.9b01010
M3 - Article
AN - SCOPUS:85082419654
SN - 2161-1653
VL - 9
SP - 494
EP - 499
JO - ACS Macro Letters
JF - ACS Macro Letters
IS - 4
ER -