158022-24-3Relevant academic research and scientific papers
Synthesis and biological evaluation of potential bisubstrate inhibitors of protein farnesyltransferase. Design and synthesis of functionalized imidazoles
De Figueiredo, Renata Marcia,Coudray, Laetitia,Dubois, Joelle
, p. 3299 - 3309 (2008/09/20)
A novel series of compounds, derived from 2,5-functionalized imidazoles, have been synthesized as potential bisubstrate inhibitors of protein farnesyltransferase (FTase) using structure-based design. These compounds have a 1,4-diacid chain and a tripeptid
Phenol-derived CVFM analog inhibitors of Ras farnesyltransferase possessing cellular in vitro activity
Caliendo, Giuseppe,Fiorino, Ferdinando,Grieco, Paolo,Perissutti, Elisa,Ramunno, Anna,Santagada, Vincenzo,Albrizio, Stefania,Califano, Daniela,Giuliano, Ada,Santelli, Giovanni
, p. 725 - 732 (2007/10/03)
A study was performed on structure-activity relationships of a series of phenol-derived, CVFM analogs, inhibitors of Ras Farnesyltransferase (FTase). The effect of various substituents on the phenol ring was examined, while the VFM moiety of the potent inhibitor CVFM was kept constant. The FTase inhibitory activity, reported as IC50 in table I, was influenced by both the chemical properties and the relative position of the substituents on the phenolic ring. The most active compounds in this series contained a chloro or bromine substituent on the phenolic ring. Subsequently we have tested the effects of these FTase inhibitors on the anchorage-dependent growth of two rat epithelial cell lines, FRTL-5 and the same line v-Ha-ras transformed. While most of the compounds were inactive, two showed a growth inhibitory effect: compound 4 was active against normal as well against transformed cells while derivative 13 was active only against transformed cells.
