Peptide C-Terminal Modification

The posttranslational modification of eukaryotic proteins by the addition of isoprenyl lipids at their C-termimi was first observed in the 1970s and 1980s. Since then, more than a hundred proteins have been shown to be modified by C15 farnesyl or C20 geranylgeranyl groups, including most members of the Ras, Rho, and Rab familied of G proteins. The C-terminal of the peptide is synthesized as an amide to neutralize negative charge created by the C-terminal COOH. This modification is added to prevent enzyme degradation, to mimic native proteins, and in some cases to remove hydrogen bonding at the C-terminal of the peptides which may interfere with the assays.

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