Labeling and Natural Post-Translational Modification of Peptides and Proteins via Chemoselective Pd-Catalyzed Prenylation of Cysteine

Thomas Schlatzer, Julia Kriegesmann, Hilmar Schröder, Melanie Trobe, Christian Lembacher-Fadum, Simone Santner, Alexander Kravchuk, Christian F. W. Becker, Rolf Breinbauer

Research output: Contribution to journalArticle

Abstract

The prenylation of peptides and proteins is an important post-translational modification observed in vivo. We report that the Pd-catalyzed Tsuji–Trost allylation with a Pd/BIPHEPHOS catalyst system allows the allylation of Cys-containing peptides and proteins with complete chemoselectivity and high n/i regioselectivity. In contrast to recently established methods, which use non-native connections, the Pd-catalyzed prenylation produces the natural n-prenylthioether bond. In addition, a variety of biophysical probes such as affinity handles and fluorescent tags can be introduced into Cys-containing peptides and proteins. Furthermore, peptides containing two cysteine residues can be stapled or cyclized using homobifunctional allylic carbonate reagents.
Original languageEnglish
Pages (from-to)14931-14937
JournalJournal of the American Chemical Society
Volume141
Issue number37
DOIs
Publication statusPublished - 2019

Keywords

  • prenylation
  • bioconjugation
  • lipidation
  • peptide cyclization
  • stapled peptides

Fields of Expertise

  • Human- & Biotechnology

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