| Literature DB >> 32991160 |
Zebediah C Girvin1, Samuel H Gellman1.
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.Mesh:
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Year: 2020 PMID: 32991160 DOI: 10.1021/jacs.0c07347
Source DB: PubMed Journal: J Am Chem Soc ISSN: 0002-7863 Impact factor: 15.419