A rationally designed aldolase foldamer

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

Research output: Contribution to journalArticle

110 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)922-925
Number of pages4
JournalAngewandte Chemie - International Edition
Volume48
Issue number5
DOIs
StatePublished - Jan 19 2009

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Fructose-Bisphosphate Aldolase
Imines
Ammonium Compounds
Peptides
Enzymes

Keywords

  • Aldol reaction
  • Enzyme models
  • Homogeneous catalysis
  • Peptides
  • Preorganization

Cite this

A rationally designed aldolase foldamer. / Müller, Manuel M.; Windsor, Matthew A.; Pomerantz, William C.; Gellman, Samuel H.; Hilvert, Donald.

In: Angewandte Chemie - International Edition, Vol. 48, No. 5, 19.01.2009, p. 922-925.

Research output: Contribution to journalArticle

Müller, MM, Windsor, MA, Pomerantz, WC, Gellman, SH & Hilvert, D 2009, 'A rationally designed aldolase foldamer', Angewandte Chemie - International Edition, vol. 48, no. 5, pp. 922-925. https://doi.org/10.1002/anie.200804996
Müller, Manuel M. ; Windsor, Matthew A. ; Pomerantz, William C. ; Gellman, Samuel H. ; Hilvert, Donald. / A rationally designed aldolase foldamer. In: Angewandte Chemie - International Edition. 2009 ; Vol. 48, No. 5. pp. 922-925.
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