Synthesis and biological evaluation of potential bisubstrate inhibitors of protein farnesyltransferase. Design and synthesis of functionalized imidazoles.

Content Provider	Semantic Scholar
Author	Figueiredo, Renata Marcia De Coudray, Laëtitia Dubois, Joëlle
Copyright Year	2007
Abstract	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 tripeptide connected by an imidazole ring. The synthetic strategy relies on the functionalization at the C-2 position of the heterocycle with the diacid side chain and peptide coupling at the C-5 position. Several new compounds were synthesized in good yields. Kinetic experiments on the most active compounds revealed different binding modes depending on the diacid chain length.
Starting Page	18
Ending Page	23
Page Count	6
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.rsc.org/suppdata/ob/b7/b709854e/b709854e.pdf
PubMed reference number	17912382v1
Volume Number	5
Issue Number	20
Journal	Organic & biomolecular chemistry
Language	English
Access Restriction	Open
Subject Keyword	Imidazoles farnesyltranstransferase protein farnesyltransferase
Content Type	Text
Resource Type	Article