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    Synthesis and Activity of Histidine-Containing Catalytic Peptide Dendrimers
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    Department of Chemistry & Biochemistry, University of Berne, Freiestrasse 3, 3012 Berne, Switzerland, and Chemspeed Technologies AG, Rheinstrasse 32, 4302 Augst, Switzerland
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    The Journal of Organic Chemistry

    Cite this: J. Org. Chem. 2006, 71, 12, 4468–4480
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    https://doi.org/10.1021/jo060273y
    Published May 6, 2006
    Copyright © 2006 American Chemical Society
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    Abstract

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    Peptide dendrimers built by iteration of the diamino acid dendron Dap-His-Ser (His = histidine, Ser = Serine, Dap = diamino propionic acid) display a strong positive dendritic effect for the catalytic hydrolysis of 8-acyloxypyrene 1,3,6-trisulfonates, which proceeds with enzyme-like kinetics in aqueous medium (Delort, E.; Darbre, T.; Reymond, J.-L. J. Am. Chem. Soc. 2004, 126, 15642−3). Thirty-two mutants of the original third generation dendrimer A3 ((Ac-His-Ser)8(Dap-His-Ser)4(Dap-His-Ser)2Dap-His-Ser-NH2) were prepared by manual synthesis or by automated synthesis with use of a Chemspeed PSW1100 peptide synthesizer. Dendrimer catalysis was specific for 8-acyloxypyrene 1,3,6-trisulfonates, and there was no activity with other types of esters. While dendrimers with hydrophobic residues at the core and histidine residues at the surface only showed weak activity, exchanging serine residues in dendrimer A3 against alanine (A3A), β-alanine (A3B), or threonine (A3C) improved catalytic efficiency. Substrate binding was correlated with the total number of histidines per dendrimer, with an average of three histidines per substrate binding site. The catalytic rate constant kcat depended on the placement of histidines within the dendrimers and the nature of the other amino acid residues. The fastest catalyst was the threonine mutant A3C ((Ac−His-Thr)8(Dap-His-Thr)4(Dap-His-Thr)2Dap-His-Thr-NH2), with kcat = 1.3 min-1, kcat/kuncat = 90‘000, KM = 160 μM for 8-bytyryloxypyrene 1,3,6-trisulfonate, corresponding to a rate acceleration of 18‘000 per catalytic site and a 5-fold improvement over the original sequence A3.

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    †

     University of Berne.

    ‡

     Chemspeed Technologies AG.

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     Address correspondence to this author. Fax:  +41 31 631 80 57.

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    Procedures for dendrimer synthesis, HPLC, and MS data of all dendrimers synthesized, procedures for kinetic measurements, and ITC and pH studies. This material is available free of charge via the Internet at http:// pubs.acs.org.

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    The Journal of Organic Chemistry

    Cite this: J. Org. Chem. 2006, 71, 12, 4468–4480
    Click to copy citationCitation copied!
    https://doi.org/10.1021/jo060273y
    Published May 6, 2006
    Copyright © 2006 American Chemical Society
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