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Foldamer Catalysis

Journal

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 142, Issue 41, Pages 17211-17223

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/jacs.0c07347

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Funding

  1. U.S. National Science Foundation [CHE-1904940]

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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.

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