Materials that can be conveniently tuned to present the bio- chemical, morphological and mechanical features of native biological systems are of special interest to the fields of biomaterials and biointerfaces. The incorporation of targeting elements minimizes the potential of negative systemic effects, an important translational consideration. These ideas have inspired significant research in peptidic biomaterials as well as the chemical functionalization of both naturally-derived and synthetic polymers. Poly(N-substituted glycine) “peptoids”, a class of highly customizable peptidomimetic macromolecules, could also potentially enable significant advances.
The biorecognition abilities of peptoids have been demon- strated through two decades of peptoid therapeutics research, protein-binding sequence discovery, and secondary structure design. Many bioactive sequences have been discovered by screening peptoid libraries.
In contrast, my research takes advantage of the synthetic accessibility and sequence programmability of peptoids for biointerfaces, materials and nanostructure engineering. Attention is focused not only on incorporating chemical functionality, but also on exploiting the mainchain flexibility of the peptoid backbone, as well as the potential of using specific residue sequences for organizing molecular functionality on the nanoscale.