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

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

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
Number of pages5
JournalOrganic & Biomolecular chemistry
Volume11
Issue number44
DOIs
Publication statusPublished - 10 Oct 2013

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