Fine Tuning the Inhibition Profile of Cyclosporine A by Derivatization of the MeBmt Residue

Authors

  • Dr. Erik Prell,

    1. Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle/Saale (Germany)
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    • These authors contributed equally to this work.

  • Viktoria Kahlert,

    1. Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle/Saale (Germany)
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    • These authors contributed equally to this work.

  • Dr. Karl Peter Rücknagel,

    1. Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle/Saale (Germany)
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  • Dr. Miroslav Malešević,

    Corresponding author
    1. Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle/Saale (Germany)
    • Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle/Saale (Germany)
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  • Prof. Gunter Fischer

    Corresponding author
    1. Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle/Saale (Germany)
    • Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle/Saale (Germany)
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Abstract

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Unique respect: The biological properties of four CsA derivatives were fine-tuned by tractable modifications of the MeBmt residue. The new CsA derivatives share strong inhibitory activity toward cyclophilins (Cyps), but each is unique with respect to immunosuppressive action and cellular localization. These CsA analogues can be used to study the physiological roles of extracellular Cyps.

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