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

Autor: Hinterding K; Institut für Organische Chemie der Universität, Richard-Willstätter-Allee 2, D-76128 Karlsruhe (Germany), Fax: (+49) 721-608-4825., Hagenbuch P; Institut für Organische Chemie der Universität, Richard-Willstätter-Allee 2, D-76128 Karlsruhe (Germany), Fax: (+49) 721-608-4825., Rétey J; Institut für Organische Chemie der Universität, Richard-Willstätter-Allee 2, D-76128 Karlsruhe (Germany), Fax: (+49) 721-608-4825., Waldmann H; Institut für Organische Chemie der Universität, Richard-Willstätter-Allee 2, D-76128 Karlsruhe (Germany), Fax: (+49) 721-608-4825.
Jazyk: angličtina
Zdroj: Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 1998 May 18; Vol. 37 (9), pp. 1236-1239.
DOI: 10.1002/(SICI)1521-3773(19980518)37:9<1236::AID-ANIE1236>3.0.CO;2-F
Abstrakt: 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 (K I = 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.
(© 1998 WILEY-VCH Verlag GmbH, Weinheim, Fed. Rep. of Germany.)
Databáze: MEDLINE
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