Last-step enzymatic [18F]-fluorination of cysteine-tethered RGD peptides using modified Barbas linkers

Qingzhi Zhang, Sergio Dall'Angelo, Ian N. Fleming, Lutz F. Schweiger, Matteo Zanda, David O'Hagan

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)
4 Downloads (Pure)


We report a last-step fluorinase-catalyzed [18F]-fluorination of a cysteine-containing RGD peptide. The peptide was attached through sulfur to a modified and more hydrophilic variant of the recently disclosed Barbas linker which was itself linked to a chloroadenosine moiety via a PEGylated chain. The fluorinase was able to use this construct as a substrate for a transhalogenation reaction to generate [18F]-radiolabeled RGD peptides, which retained high affinity to cancer-cell relevant αvβ3 integrins.
Original languageEnglish
Pages (from-to)10998–11004
JournalChemistry - A European Journal
Issue number31
Early online date4 Jul 2016
Publication statusPublished - 25 Jul 2016


  • 18F labeling
  • Barbas linker
  • Bioconjugation
  • Chemical biology
  • RGD peptide


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