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Issue 17, 2006
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Artificial aldolases from peptide dendrimer combinatorial libraries

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Abstract

Peptide dendrimers were investigated as synthetic models for aldolase enzymes. Combinatorial libraries were prepared with aldolase active residues such as lysine and proline placed at the dendrimer core or near the surface. On-bead selection for aldolase activity was carried out using the dye-labelled 1,3-diketone 1a, suitable for covalent trapping of enamine-reactive side-chains, and the fluorogenic enolization probe 6. Aldolase dendrimers catalyzed the aldol reaction of acetone, dihydroxyacetone and cyclohexanone with nitrobenzaldehyde. Much like enzymes, the dendrimers exhibited strong aldolase activity in aqueous medium, but were also active in organic solvent. Dendrimer-catalyzed aldol reactions reached complete conversion in 3 h at 25 °C with 1 mol% catalyst and gave aldol products with up to 65% ee. A positive dendritic effect in catalysis was observed with both lysine and proline based aldolase dendrimer catalysts.

Graphical abstract: Artificial aldolases from peptide dendrimer combinatorial libraries

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Supplementary files

Article information


Submitted
23 May 2006
Accepted
05 Jul 2006
First published
26 Jul 2006

Org. Biomol. Chem., 2006,4, 3268-3281
Article type
Paper

Artificial aldolases from peptide dendrimer combinatorial libraries

J. Kofoed, T. Darbre and J. Reymond, Org. Biomol. Chem., 2006, 4, 3268
DOI: 10.1039/B607342E

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