Projects per year
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 language | English |
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Pages (from-to) | 14931-14937 |
Journal | Journal of the American Chemical Society |
Volume | 141 |
Issue number | 37 |
DOIs | |
Publication status | Published - 2019 |
Keywords
- prenylation
- bioconjugation
- lipidation
- peptide cyclization
- stapled peptides
Fields of Expertise
- Human- & Biotechnology
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Dive into the research topics of 'Labeling and Natural Post-Translational Modification of Peptides and Proteins via Chemoselective Pd-Catalyzed Prenylation of Cysteine'. Together they form a unique fingerprint.Projects
- 1 Finished
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FWF - Peptide - Transition-metal catalyzed post-translational modification of peptides and proteins
1/09/16 → 31/07/21
Project: Research project