Premium
Solid‐Phase Synthesis and Biological Evaluation of a Pepticinnamin E Library
Author(s) -
Thutewohl Michael,
Kissau Lars,
Popkirova Boriana,
Karaguni IonnaMaria,
Nowak Thorsten,
Bate Michael,
Kuhlmann Jürgen,
Müller Oliver,
Waldmann Herbert
Publication year - 2002
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 - 10.1002/1521-3773(20021004)41:19<3616::aid-anie3616>3.0.co;2-f
Subject(s) - farnesyltransferase , natural product , peptide , tumor cells , chemistry , computational biology , peptide synthesis , enzyme , biochemistry , combinatorial chemistry , library science , computer science , stereochemistry , information retrieval , biology , cancer research , prenylation
Potent mono‐ and bisubstrate inhibitors of the enzyme protein farnesyltransferase are furnished by a structurally broadly varied compound library derived from the natural product pepticinnamin E (see picture), by a six‐to‐nine‐step solid‐phase peptide synthesis. One inhibitor was identified as inducing apoptosis in H‐Ras‐transformed tumor cells.