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Issue 20, 2011
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Peptide dendrimer enzyme models for ester hydrolysis 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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Publication details

The article was received on 02 Jun 2011, accepted on 20 Jul 2011 and first published on 30 Aug 2011


Article type: Paper
DOI: 10.1039/C1OB05877K
Citation: Org. Biomol. Chem., 2011,9, 7071-7084
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    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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