2. Academic Validation
  3. Synthesis and In Vitro Evaluation of the Ras Farnesyltransferase Inhibitor Pepticinnamin E

Synthesis and In Vitro Evaluation of the Ras Farnesyltransferase Inhibitor Pepticinnamin E

  • Angew Chem Int Ed Engl. 1998 May 18;37(9):1236-1239. doi: 10.1002/(SICI)1521-3773(19980518)37:9<1236::AID-ANIE1236>3.0.CO;2-F.
Klaus Hinterding 1,  Patrizia Hagenbuch 1,  Janos Rétey 1,  Herbert Waldmann 1
Affiliations

Affiliation

  • 1 Institut für Organische Chemie der Universität, Richard-Willstätter-Allee 2, D-76128 Karlsruhe (Germany), Fax: (+49) 721-608-4825.
PMID: 29711232 DOI: 10.1002/(SICI)1521-3773(19980518)37:9<1236::AID-ANIE1236>3.0.CO;2-F
Abstract

A modularly built bisubstrate inhibitor, the natural product pepticinnamin E (shown on the right) was sythesized for the first time. In the case of in vitro assays it inhibits the Enzyme farnesyltransferase with respect to both the peptide substrate and farnesylpyrophosphate (KI = 30 and 8 μM, respectively). The inhibitory activity is decisively influenced by the central tripeptide unit and the absolute configuration of the non-proteinogenic amino acid incorporated therein.

Keywords

Bioorganic chemistry; Enzyme inhibitors; Pepticinnamin E; Signal transduction.

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