Solid-phase synthesis of a pepticinnamin E library.
Pepticinnamin E is a naturally occurring bisubstrate inhibitor of farnesyltransferase. Based on the structure of the natural product, a compound library was synthesized by variation of eight structural parameters. Following three different routes, a total of 51 analogues was synthesized on the polymeric support in 6-11-step parallel syntheses. Overall yields ranged from 3 to 63%, and the compounds were obtained with >90% purity.
Thutewohl
Michael
M
Max-Planck-Institut für molekulare Physiologie, Abt. Chemische Biologie, Otto-Hahn-Str. 11, D-44227, Organische Chemie, Universität Dortmund, Dortmund und Fachbereich 3, Germany
Waldmann
Herbert
H
D019883:Alkyl and Aryl Transferases / Q000037:antagonists & inhibitors / Q000378:metabolism; D004791:Enzyme Inhibitors / Q000138:chemical synthesis / Q000494:pharmacology; D051231:Farnesyltranstransferase; D020128:Inhibitory Concentration 50; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D019151:Peptide Library; D018631:ras Proteins / Q000378:metabolism
D004791:Enzyme Inhibitors; D009842:Oligopeptides; D019151:Peptide Library; C080552:pepticinnamin E; D019883:Alkyl and Aryl Transferases; D051231:Farnesyltranstransferase; D018631:ras Proteins