Enzymatic incorporation of orthogonally reactive prenylazide groups into peptides using geranylazide diphosphate via protein farnesyltransferase: Implications for selective protein labeling

Matthew W. Rose, Juhua Xu, Tamara A. Kale, George O'Doherty, George Barany, Mark D. Distefano

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

Protein farnesyltransferase (PFTase) catalyzes the attachment of a geranyl azide moiety to apeptide substrate, N-dansyl-Gly-Cys-Val-Ile-Ala-OH. The resulting azide-containing peptide was derivatized with a triphenylphosphine- based reagent to generate an O-alkyl imidate-linked product, rather than the amide-linked material expected via a Staudinger reaction. Since the CAAX box recognition motif (where the internal A residues are aliphatic amino acids) modified by PFTase can be incorporated into the C-terminus of virtually any polypeptide, this two-step procedure provides a general method for incorporating a diverse range of chemical modifications specifically near the C-terminus of proteins.

Original languageEnglish (US)
Pages (from-to)164-171
Number of pages8
JournalBiopolymers - Peptide Science Section
Volume80
Issue number2-3
DOIs
StatePublished - Jun 20 2005

Keywords

  • CAAX box
  • Cysteine modification
  • Farnesyltransferase
  • Geranyl azide
  • Prenyl azide
  • Prenylated peptides
  • Selective peptide modification
  • Staudinger ligation

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