A rationally designed aldolase foldamer

Manuel M. Müller; Matthew A. Windsor; William C. Pomerantz; Samuel H. Gellman; Donald Hilvert

doi:10.1002/anie.200804996

A rationally designed aldolase foldamer

Manuel M. Müller, Matthew A. Windsor, William C. Pomerantz, Samuel H. Gellman, Donald Hilvert

Chemistry (Twin Cities)

Research output: Contribution to journal › Article › peer-review

143 Scopus citations

Abstract

(Chemical Equation Presented) 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.

Original language	English (US)
Pages (from-to)	922-925
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	48
Issue number	5
DOIs	https://doi.org/10.1002/anie.200804996
State	Published - Jan 19 2009

Keywords

Aldol reaction
Enzyme models
Homogeneous catalysis
Peptides
Preorganization

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KW - Homogeneous catalysis

KW - Peptides

KW - Preorganization

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A rationally designed aldolase foldamer

Abstract

Keywords

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