A Rationally Designed Aldolase Foldamer

Authors


  • This work was supported by the Schweizerischer Nationalfonds, NIH grant GM056414 (to S.H.G.), and the Nanoscale Science and Engineering Center at UW-Madison (NSF DMR-042588). We thank Dr. Dennis Gillingham for help with substrate preparation.

Abstract

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Neatly folded: A decameric β-peptide shows enzyme-like catalytic properties. The foldamer, which bears a terminal heptanoyl unit and displays a thermostable helical structure with an array of ammonium-group side chains, accelerates a retroaldol reaction (see scheme) by more than three orders of magnitude through an imine mechanism.

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