Pepticinnamins, new farnesyl-protein transferase inhibitors produced by an actinomycete. I. Producing strain, fermentation, isolation and biological activity.
Pepticinnamins A, B, C, D, E and F, a family of farnesyl-protein transferase (FPT) inhibitors were isolated from the fermentation broth of Streptomyces sp. OH-4652. These inhibitors were purified from whole broth by extraction with chloroform, followed by silica gel column chromatography, Sephadex LH-20 chromatography and reverse phase HPLC. Among these, pepticinnamin C showed the most potent inhibition (IC50-100 nM).
Omura
S
S
Research Center for Biological Function, Kitasato Institute, Tokyo, Japan.
Van der Pyl
D
D
Inokoshi
J
J
Takahashi
Y
Y
Takeshima
H
H
D019883:Alkyl and Aryl Transferases; D000818:Animals; D001419:Bacteria / Q000187:drug effects; D002455:Cell Division / Q000187:drug effects; D004791:Enzyme Inhibitors / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology; D005285:Fermentation; D008826:Microbial Sensitivity Tests; D009842:Oligopeptides / Q000096:biosynthesis / Q000302:isolation & purification* / Q000494:pharmacology; D013302:Streptomyces / Q000145:classification / Q000378:metabolism*; D014166:Transferases / Q000037:antagonists & inhibitors*; D014709:Vero Cells
D004791:Enzyme Inhibitors; D009842:Oligopeptides; C080552:pepticinnamin E; D014166:Transferases; D019883:Alkyl and Aryl Transferases; C064911:p21(ras) farnesyl-protein transferase