Triazole biotin: a tight-binding biotinidase-resistant conjugate

Anne I. Germeroth, Jill R. Hanna, Rehana Karim, Franziska Kundel, Jonathan Lowther, Peter G. N. Neate, Elizabeth A. Blackburn, Martin A. Wear, Dominic J. Campopiano, Alison N. Hulme

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    The natural amide bond found in all biotinylated proteins has been replaced with a triazole through CuAAC reaction of an alkynyl biotin derivative. The resultant triazole-linked adducts are shown to be highly resistant to the ubiquitous hydrolytic enzyme biotinidase and to bind avidin with dissociation constants in the low pM range. Application of this strategy to the production of a series of biotinidase-resistant biotin-Gd-DOTA contrast agents is demonstrated.

    Original languageEnglish
    Pages (from-to)7700-7704
    JournalOrganic and Biomolecular Chemistry
    Issue number44
    Publication statusPublished - 1 Jan 2013


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