Inhibition of Ras prenylation: A signaling target for novel anti-cancer drug design

Edwina C. Lerner, Andrew D. Hamilton, Saïd M. Sebti

Research output: Contribution to journalReview articlepeer-review


The cancer-causing activity of Ras requires the prenylation of a cysteine fourth from its carboxyl terminus. Rational design of peptidomimetics of the carboxyl terminal tetrapeptide prenylation site on Ras resulted in pharmacological agents capable of inhibiting Ras processing, selectively antagonizing oncogenic signaling and suppressing human tumor growth in mouse models without side effects. This mini-review describes the efforts of several groups to design, synthesize and evaluate the biological activities of farnesyltransferase and geranylgeranyltransferase I inhibitors. Among the important issues that will be discussed are the mechanism of action of these inhibitors and the potential mechanisms of resistance to inhibition of K-Ras farnesylation.

Original languageEnglish (US)
Pages (from-to)229-238
Number of pages10
JournalAnti-Cancer Drug Design
Issue number4
StatePublished - Jun 1997

ASJC Scopus subject areas

  • Biochemistry
  • Oncology
  • General Biochemistry, Genetics and Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Organic Chemistry


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