Peptoids are biomimetic derivatives of proteins that potentially expand the structural and functional repertoire of proteins while being impervious to biological degradation. Despite the potential utility of peptoids in novel medical and industrial settings, little is known about the basic rules and design criteria that dictate the formation of peptoid structure. Here we focus on a recently discovered peptoid nanomaterial: a nanosheet bilayer-that is unavailable to analogous peptides, and hence serves as a lesson in how the natural repertoire of peptides may be expanded with the help of peptoids. We report the the first atom-resolution structure of a peptoid bilayer, obtained from molecular dynamics. These closely match the nanoscale structure obtained from experiment (x-ray scattering, atomic force microscopy). Simulations also reveal unexpected features of nanosheets, such as their possible water-porosity. More generally, backbone dihedral angles indicate how the lack of chirality to the backbone carbon atoms permits the bilayer to extend to mesoscopic scales. These findings indicate a distinct but complementary ruleset that may be employed for the development of tertiary peptoid configurations that are not permitted in the chiral peptide world.Figure 1. Side-view of a peptoid bilayer from molecular dynamics.

Design criteria of novel protein-mimetic polymers from simulation

248th National Meeting (2014)

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