PerspectiveOrganic Chemistry

Peptidic catalysts for macrocycle synthesis

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Science  20 Dec 2019:
Vol. 366, Issue 6472, pp. 1454
DOI: 10.1126/science.aaz9325

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Summary

Many structurally simplified catalysts have been synthesized that mimic the reactivity and efficiency of enzymes. In this context, the numerous transformations catalyzed by the amino acid proline as a catalytic-site mimic helped drive the field of organocatalysis (1). Enzyme activity not only relies on the reactive site but also on the structure of the binding pocket that can orient and twist substrates for reactions. Oligopeptide catalysts, often referred to as foldamers (2), can emulate both the reactivity and substrate positioning and folding of enzymes by using the secondary peptide structure such as α-helices or β-turns. On page 1528 of this issue, Girvin et al. (3) translate enzymatic synthesis of large rings (macrocycles) into a heptapeptide foldamer catalyst that performs an intramolecular aldol condensation (see the figure).

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