Synthesis of prenylated peptides and peptide esters

✍ Scribed by Fred R. Naider; Jeffrey M. Becker

• Publisher: Wiley (John Wiley & Sons)
• Year: 1997
• Tongue: English
• Weight: 116 KB
• Volume: 43
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/(sici)1097-0282(1997)43:1<3::aid-bip2>3.0.co;2-z

✦ Synopsis

Modification of the cysteine sulfur in peptides and proteins to a thioether is a recently described posttranslational event that results in the incorporation of farnesyl and geranylgeranyl moieties. The increased lipophilicity accompanying these modifications often causes localization of the resulting protein to the membrane and may be essential for biological activity. Methods are described to chemically and biochemically synthesize farnesylated and geranylgeranylated peptides and proteins from microgram to gram quantities. Conditions for thioalkylation include acidic, neutral, and basic media. The ability to readily form peptidylthioethers will greatly facilitate studies of biologically important proteins and peptides containing isoprenyl moieties.