Premium
Synthesis and In Vitro Evaluation of the Ras Farnesyltransferase Inhibitor Pepticinnamin E
Author(s) -
Hinterding Klaus,
Hagenbuch Patrizia,
Rétey Janos,
Waldmann Herbert
Publication year - 1998
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/(sici)1521-3773(19980518)37:9<1236::aid-anie1236>3.0.co;2-f
Subject(s) - farnesyltransferase , tripeptide , farnesyltransferase inhibitor , in vitro , natural product , chemistry , enzyme , biochemistry , amino acid , substrate (aquarium) , peptide , stereochemistry , biology , prenylation , ecology
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 μ M , respectively). The inhibitory activity is decisively influenced by the central tripeptide unit and the absolute configuration of the non‐proteinogenic amino acid incorporated therein.