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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Benzodiazepine peptidomimetics: potent inhibitors of Ras farnesylation in animal cells.

Oncogenic Ras proteins transform animal cells to a malignant phenotype only when modified by farnesyl residues attached to cysteines near their carboxyl termini. The farnesyltransferase that catalyzes this reaction recognizes tetrapeptides of the sequence CAAX, where C is cysteine, A is an aliphatic amino acid, and X is a carboxyl-terminal methionine or serine. Replacement of the two aliphatic residues with a benzodiazepine-based mimic of a peptide turn generated potent inhibitors of farnesyltransferase [50 percent inhibitory concentration (IC50) < 1 nM]. Unlike tetrapeptides, the benzodiazepine peptidomimetics enter cells and block attachment of farnesyl to Ras, nuclear lamins, and several other proteins. At micromolar concentrations, these inhibitors restored a normal growth pattern to Ras-transformed cells. The benzodiazepine peptidomimetics may be useful in the design of treatments for tumors in which oncogenic Ras proteins contribute to abnormal growth, such as that of the colon, lung, and pancreas.[1]


  1. Benzodiazepine peptidomimetics: potent inhibitors of Ras farnesylation in animal cells. James, G.L., Goldstein, J.L., Brown, M.S., Rawson, T.E., Somers, T.C., McDowell, R.S., Crowley, C.W., Lucas, B.K., Levinson, A.D., Marsters, J.C. Science (1993) [Pubmed]
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