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Design, synthesis, and evaluation of potent and selective benzoyleneurea-based inhibitors of protein geranylgeranyltransferase-I
- 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.
- Subjects :
- Models, Molecular
Magnetic Resonance Spectroscopy
Peptidomimetic
Stereochemistry
Farnesyltransferase
Clinical Biochemistry
Pharmaceutical Science
Biochemistry
Chemical synthesis
Mass Spectrometry
chemistry.chemical_compound
Drug Discovery
Animals
Urea
Enzyme Inhibitors
Molecular Biology
IC50
chemistry.chemical_classification
Dipeptide
Alkyl and Aryl Transferases
biology
Molecular Structure
Organic Chemistry
In vitro
Enzyme
chemistry
Enzyme inhibitor
Drug Design
biology.protein
Molecular Medicine
Subjects
Details
- ISSN :
- 09680896
- Volume :
- 13
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- Bioorganicmedicinal chemistry
- Accession number :
- edsair.doi.dedup.....482d9145c46182c6ca55926749454c7a