Exploration of\nTertiary Structure in Sequence-Defined\nPolymers Using Molecular Dynamics Simulations

Peptoids are a class of sequence-defined biomimetic polymers\nwith\npeptide-like backbones and side chains located on backbone nitrogens\nrather than alpha carbons. These materials demonstrate a strong ability\nfor precise control of single-chain structure, multiunit self-assembly,\nand macromolecular assembly through careful tuning of sequence due\nto the diversity of available side chains, although the driving forces\nbehind these assemblies are often not understood. Prior experimental\nwork has shown that linked 15mer peptoids can mimic the protein helical\nhairpin structure by leveraging the chirality-inducing nature of bulky\nside chains and hydrophobicity, but there are still gaps in our understanding\nof the relationship between sequence, stability, and particular secondary\nor tertiary structure. We present a molecular dynamics (MD) study\non the folding behavior of these polymers into hairpins, discussing\nthe differences in structure from sequences with various characteristics\nin water and acetonitrile, and then compare the handedness preference\nof common helical motifs between solvents.