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Pseudodipeptide Inhibitors of Protein Farnesyltransferase
de Solms, S. Jane,Deana, Albert A.,Giuliani, Elizabeth A.,Graham, Samuel L.,Kohl, Nancy E.,et al.
, p. 3967 - 3971 (2007/10/03)
A series of pseudodipeptide amides are described that inhibit Ras protein farnesyltransferase (PFTase).These inhibitors are truncated versions of the C-terminal tetrapeptide (CAAX motif) of Ras that serves as the signal sequence for PFTase-catalyzed protein farnesylation.In contrast to CAAX peptidomimetics previously reported, these inhibitors do not have a C-terminal carboxyl moiety, yet they inhibit farnesylation in vitro at 100 nM.Despite the absence of the X residue in the CAAX motif, which normally directs prenylation specificity, these pseudodipeptides are greater than 100-fold selective for PFTase over type 1 protein geranylgeranyltransferase.
