Foldamer Catalysis

Abstract

The extraordinary rate accelerations and control of reactivity exhibited by enzymes have long inspired efforts to develop synthetic catalysts. Foldamers, which are oligomers with a strong tendency to adopt a specific conformation, represent unique platforms for efforts to harness principles of enzyme function for catalyst design. Well-defined helical structures that have been identified in several foldamer families can serve as scaffolds for the predictable spatial arrangement of functional groups. The chirality of these helices offers a basis for asymmetric catalysis. Thus, foldamer-based approaches to catalyst development represent an attractive alternative to well-developed strategies involving small molecules or conventional peptides.