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Design, synthesis, and evaluation of potent and selective benzoyleneurea-based inhibitors of protein geranylgeranyltransferase-I

Authors :
Andrew D. Hamilton
Dora Carrico
Cynthia Bucher
Michelle A. Blaskovich
Said M. Sebti
Source :
Bioorganicmedicinal chemistry. 13(3)
Publication Year :
2004

Abstract

A series of novel protein geranylgeranyltransferase-I (PGGTase-I) inhibitors based on a benzoyleneurea scaffold has been synthesized. Using a benzoyleneurea scaffold as a mimetic for the central dipeptide (AA), we have developed CAAX peptidomimetic inhibitors that selectively block the activity of PGGTase-I over the closely related enzyme protein farnesyltransferase. In this new class of PGGTase-I inhibitors, compound (6c) with X=L-phenylalanine, displayed the highest inhibition activity against PGGTase-I with an IC50 value of 170 nM. The inhibitors described in this study represent novel and promising leads for the development of potent and selective inhibitors of mammalian PGGTase-I for potential application as antitumor agents.

Details

ISSN :
09680896
Volume :
13
Issue :
3
Database :
OpenAIRE
Journal :
Bioorganicmedicinal chemistry
Accession number :
edsair.doi.dedup.....482d9145c46182c6ca55926749454c7a