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 language | English (US) |
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Pages (from-to) | 164-171 |
Number of pages | 8 |
Journal | Biopolymers - Peptide Science Section |
Volume | 80 |
Issue number | 2-3 |
DOIs | |
State | Published - 2005 |
Keywords
- CAAX box
- Cysteine modification
- Farnesyltransferase
- Geranyl azide
- Prenyl azide
- Prenylated peptides
- Selective peptide modification
- Staudinger ligation