Peptoids, oligomers of N-substituted glycine, are useful biomimetic polymers. To date, examples of peptoids that mimic protein secondary structural motifs (helices, turns, ribbons) have been reported, but very few peptoids exhibit higher order structures that rival the complexity of biomolecular structure. We have prepared and studied water-soluble peptoids that can self-associate. Peptoids comprise the strongly helix-promoting residue N-S-(1-naphthylethyl)glycine (Ns1npe), which is intrinsically fluorescent. CD spectroscopy, fluorescence spectroscopy, and other techniques have been used to explore the influence of a peptoid's sequence on its propensity to self-associate in water, and spectral features have been correlated with more robust association. Our data are consistent with a hydrophobically-driven self-associative mechanism. Peptoid length, secondary structure, and amphiphilicity all influence aggregation. These results enhance the existing understanding of peptoid sequence-structure relationships, and such peptoids have potential promising applications as sensors or sequestrants. 

Synthesis and structural evaluation of self-associating water-soluble peptoids

248th National Meeting (2014)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.