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Issue 20, 2011
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Peptidedendrimerenzyme models for esterhydrolysis and aldolization prepared by convergent thioether ligation

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Abstract

Peptide dendrimers with multiple histidines or N-terminal prolines efficiently catalyze ester hydrolysis or aldol reactions in aqueous medium. Part of the catalytic proficiency of these dendritic enzyme models stems from multivalency effects observed in G2, G3 and G4 dendrimers displaying multiple catalytic groups in their branches. To study multivalency in higher generation systems, G4, G5 and G6 peptide dendrimers were prepared by a convergent assembly. Thus, peptide dendrimers bearing four or eight chloroacetyl groups at their N-termini underwent multiple thioether ligation with G2 and G3 peptide dendrimers with a cysteine residue at their focal point, to give G4, G5 and G6 dendrimers containing up to 341 amino acids, including multiple histidines or N-terminal prolines. While the efficiency of the esterase catalysts was comparable to that of their lower generation analogs, a remarkable reactivity increase was observed in G5 and G6 aldolase dendrimers.

Graphical abstract: Peptide dendrimer enzyme models for ester hydrolysis and aldolization prepared by convergent thioether ligation

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Supplementary files

Article information


Submitted
02 Jun 2011
Accepted
20 Jul 2011
First published
30 Aug 2011

Org. Biomol. Chem., 2011,9, 7071-7084
Article type
Paper

Peptide dendrimer enzyme models for ester hydrolysis and aldolization prepared by convergent thioether ligation

N. A. Uhlich, T. Darbre and J. Reymond, Org. Biomol. Chem., 2011, 9, 7071
DOI: 10.1039/C1OB05877K

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