Nature uses sequence-defined polymers such as polypeptides to create biomaterials, encode information, perform biocatalysis, participate in molecular recognition, and shuttle species across membranes. Efforts to mimic nature typically utilize amino acids and amino acid derivatives to form peptidomimetics having amide bonds.Presented here is a new class of synthetic sequence-defined polymers which do not use peptide bonds. Utilizing a triazine core, side groups are readily introduced, and polymers formed by solid phase synthesis.

Thus, multiple reactive sites are utilized that can be sequentially acted upon in a pre-determined, well-controlled manner to create molecular precursors or submonomers. This sequential reactivity provides advancement over prior methods used to form conventional sequence-defined peptide polymers because it provides completely new polymeric architectures, as compared to conventional peptide, peptoid, or nucleic acid polymers.

Molecular dynamics simulations can be used to determine the forces and/or interactions that govern folding and assembly of the polymers. The simulations show conformational order due to hydrogen bonding and other interactions illustrative of protein secondary structure. Side chain functionality, self-organizing conformations, and intermolecular self-assembly of TZPs may lead to biomimetic functionality and applications.