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Oriented Immobilization of Farnesylated Proteins by the Thiol-Ene Reaction

Authors

  • Dirk Weinrich Dr.,

    1. Abteilung für Chemische Biologie, Max-Planck-Institut für Molekulare Physiologie, Otto-Hahn-Strasse 11, 44227 Dortmund (Germany)
    2. Fakultät Chemie, Chemische Biologie, Technische Universität Dortmund, Otto-Hahn-Strasse 6, 44227 Dortmund (Germany), Fax: (+49) 231-133-2499
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  • Po-Chiao Lin Dr.,

    1. Abteilung für Chemische Biologie, Max-Planck-Institut für Molekulare Physiologie, Otto-Hahn-Strasse 11, 44227 Dortmund (Germany)
    2. Fakultät Chemie, Chemische Biologie, Technische Universität Dortmund, Otto-Hahn-Strasse 6, 44227 Dortmund (Germany), Fax: (+49) 231-133-2499
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  • Pascal Jonkheijm Dr.,

    1. MESA+ Institute for Nanotechnology, University of Twente (Netherlands)
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  • Uyen T. T. Nguyen Dr.,

    1. Abteilung für Physikalische Biochemie, Max-Planck-Institut für Molekulare Physiologie (Germany)
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  • Hendrik Schröder Dr.,

    1. Fakultät Chemie, Biologisch-Chemische Mikrostrukturtechnik, Technische Universität Dortmund (Germany)
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  • Christof M. Niemeyer Prof. Dr.,

    1. Fakultät Chemie, Biologisch-Chemische Mikrostrukturtechnik, Technische Universität Dortmund (Germany)
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  • Kirill Alexandrov Prof. Dr.,

    1. Institute for Molecular Bioscience, The University of Queensland, St Lucia QLD 4072 (Australia)
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  • Roger Goody Prof. Dr.,

    1. Abteilung für Physikalische Biochemie, Max-Planck-Institut für Molekulare Physiologie (Germany)
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  • Herbert Waldmann Prof. Dr.

    1. Abteilung für Chemische Biologie, Max-Planck-Institut für Molekulare Physiologie, Otto-Hahn-Strasse 11, 44227 Dortmund (Germany)
    2. Fakultät Chemie, Chemische Biologie, Technische Universität Dortmund, Otto-Hahn-Strasse 6, 44227 Dortmund (Germany), Fax: (+49) 231-133-2499
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  • This research was supported by the Deutsche Forschungsgemeinschaft and the Fonds der Chemischen Industrie. It was also supported in part by Deutsche Forschungsgemeinschaft grant AL 484/5-4 and a Heisenberg Fellowship to K.A.

Abstract

original image

Anchoring the protein: Proteins were immobilized rapidly under mild conditions by thiol-ene photocoupling between S-farnesyl groups attached to a genetically encodable “CAAX-box” tetrapeptide sequence (A is aliphatic) at the C terminus of the protein and surface-exposed thiols (see scheme). This method enables the oriented covalent immobilization of proteins directly from expression lysates without additional purification or derivatization steps.

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