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Synthesis and in vitro evaluation of the farnesyltransferase inhibitor pepticinnamin E

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons98735

Waldmann,  Herbert
Abt. IV: Chemische Biologie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Citation

Hinterding, K., Hagenbuch, P., Retey, J., & Waldmann, H. (1999). Synthesis and in vitro evaluation of the farnesyltransferase inhibitor pepticinnamin E. CHEMISTRY-A EUROPEAN JOURNAL, 5(1), 227-236. doi:10.1002/(SICI)1521-3765(19990104)5:1<227:AID-CHEM227>3.0.CO;2-X.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0014-7130-0
Abstract
The farnesyltransferase inhibitor pepticinnamin E was synthesized and shown to have the S configuration at the central, non-proteinogenic amino acid. Using a recombinant yeast farnesyltransferase the biological activity of the natural product and structural analogues was determined. It was shown that pepticinnamin E is a bisubstrate inhibitor. Furthermore, several structural parameters were identified that decisively influence inhibition of the farnesyl transfer.