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Enzymatic Cyclisation of Peptides with a Transglutaminase

Authors

  • Jeremy Touati,

    1. Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne, 1015 Lausanne (Switzerland)
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  • Dr. Alessandro Angelini,

    1. Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne, 1015 Lausanne (Switzerland)
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  • Dr. Marlon J. Hinner,

    1. Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne, 1015 Lausanne (Switzerland)
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  • Prof. Dr. Christian Heinis

    Corresponding author
    1. Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne, 1015 Lausanne (Switzerland)
    • Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne, 1015 Lausanne (Switzerland)
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Abstract

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The ability of microbial transglutaminase to ligate two polypeptides through glutamine and lysine residues was exploited to generate cyclic peptides. Peptides with an N-terminal short glutamine-donor sequence (Ala-Leu-Gln), a variable polypeptide linker and a C-terminal lysine residue could efficiently be cyclised by the enzyme.

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