Sequence-specific “peptoids” for antifouling, antibacterial and self-assembly applications

Analogous to peptides, non-natural poly(N-substituted glycine) “peptoids” exhibit self-assembly properties and bioactivity that are encoded by the ordering of monomer residues into specific sequences along their polymer backbone. Peptoids differ from peptides in the shift of the sidechain attachment to the backbone amide-nitrogen atoms. They are resistant to protease degradation and have simplified intermolecular interactions.

This webinar highlights recent efforts in exploring solid-phase synthesized peptoids for applications beyond their conventional use in combinatorial drug discovery. The featured speaker will showcase a series of novel properties including the shortest peptoid motifs found to self-assemble into micelles and nanofibrils, “stealth” surface-grafted peptoid brushes that resist biofouling, as well as the modification of known sequences to retain antimicrobial activity for biomedical surface applications. Preliminary results also show that self-assembled peptoid nanosheets can influence protein expression of stem cells under culture. Selected peptoids have been synthesized with a Prelude^® X peptide synthesizer.