Enzymatic incorporation of orthogonally reactive prenylazide groups into peptides using geranylazide diphosphate via protein farnesyltransferase: Implications for selective protein labeling
✍ Scribed by Matthew W. Rose; Juhua Xu; Tamara A. Kale; George O'Doherty; George Barany; Mark D. Distefano
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2005
- Tongue
- English
- Weight
- 128 KB
- Volume
- 80
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
Protein farnesyltransferase (PFTase) catalyzes the attachment of a geranyl azide moiety to a peptide 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. © 2005 Wiley Periodicals, Inc. Biopolymers (Pept Sci), 2005