Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 141, Issue 37, Pages 14931-14937Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.9b08279
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Funding
- Austrian Science Fund (FWF) [P29458]
- University of Vienna
- NAWI Graz
- Austrian Science Fund (FWF) [P29458] Funding Source: Austrian Science Fund (FWF)
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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 Cyscontaining 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-prenyl-thioether 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.
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