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.
Zebediah C Girvin, Samuel H Gellman. Foldamer Catalysis. Journal of the American Chemical Society. 2020 Oct 14;142(41):17211-17223
PMID: 32991160
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