Peptoid oligomers are incapable of forming backbone hydrogen bond networks, and may therefore be anticipated to exhibit substantial conformational heterogeneity. Nevertheless, a variety of strategies have now been described to identify peptoid side chains that can enforce local conformational ordering. In addition, long-range conformational constraints can be established by macrocyclization. These strategies permit the development of predictable sequence-structure-function relationships, and peptoids can now be considered one of the prototypical examples of foldamer molecules. Control of peptoid primary sequence permits the design of oligomers that function as antifreeze agents and as scaffolds for bioactive multivalent displays. Control of peptoid secondary structure permits the design of potent antimicrobial agents, along with supramolecular assemblies such as peptoid nanotubes that reversibly sequester water molecules. A rudimentary peptoid tertiary structure has been attained by the tethered packing of peptoid macrocycles (Figure 1 ). Future rational design will increasingly be propelled by development of computational tools for accurate prediction of peptoid structure. These advances may enable the design of folded synthetic polymers that recapitulate the structural complexity and functional sophistication of biopolymers.Figure  1  . X-ray crystal structure of a rudimentary peptoid tertiary structure assembled by covalent tethering of oligomer macrocycles. Side chains are omitted for clarity.

Developing sequence-structure-function relationships in peptoid oligomers

247th National Meeting (2014)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.