343305-88-4

Basic information

• Product Name: N-[2-[3-benzoyl-4-[(4-methylphenyl)acetylamino]phenyl]]-N^α-tert-butyloxycarbonylglycine amide
• Synonyms: N-[2-[3-benzoyl-4-[(4-methylphenyl)acetylamino]phenyl]]-N^α-tert-butyloxycarbonylglycine amide
• CAS NO: 343305-88-4
• Molecular Weight: 501.582
• Mol File: 343305-88-4.mol
• Article Data: 3

Chemical Properties

• CAS DataBase Reference: N-[2-[3-benzoyl-4-[(4-methylphenyl)acetylamino]phenyl]]-N^α-tert-butyloxycarbonylglycine amide(CAS DataBase Reference)
• NIST Chemistry Reference: N-[2-[3-benzoyl-4-[(4-methylphenyl)acetylamino]phenyl]]-N^α-tert-butyloxycarbonylglycine amide(343305-88-4)
• EPA Substance Registry System: N-[2-[3-benzoyl-4-[(4-methylphenyl)acetylamino]phenyl]]-N^α-tert-butyloxycarbonylglycine amide(343305-88-4)

Safety Data

• Hazardous Substances Data: 343305-88-4(Hazardous Substances Data)

Upstream product

• 66866-43-1 N-(t-butoxycarbonyl)glycyl i-butyl carbonate 
• 265648-28-0 N-(4-amino-2-benzoylphenyl)-2-(4-methylphenyl)acetic acid amide 
• 4530-20-5 BOC-glycine 

Relevant articles and documents

Non-thiol farnesyltransferase inhibitors: Structure-activity relationships of aralkylsubsituted benzophenones

We describe a novel class of benzophenone-based farnesyltransferase inhibitors exploiting a novel aryl binding region in the farnesyltransferase's active site. The present study was mainly focussed on structural modifications of the trimethylene spacer of the 4-phenyl butyroyl residue of our lead structure (IC50 = 530 nM). These modifications turned out to have little effect on activity as had the replacement of the terminal aryl by cyclohexyl (IC50 = 440 nM vs. IC50 = 530 nM).

Non-thiol farnesyltransferase inhibitors: structure-activity relationships of benzophenone-based bisubstrate analogue farnesyltransferase inhibitors.

Investigations on the structure-activity relationships of benzophenone-based bisubstrate analogue farnesyltransferase inhibitors yielded a bisubstrate analogue farnesyltransferase inhibitor lacking any prenylic or peptidic substructures with nanomolar activity. This represents a considerable progress in comparison to those non-prenylic, non-peptidic bisubstrate analogue farnesyltransferase inhibitors we have described before which utilized AAX-peptidomimetic substructures different from the benzophenone since those inhibitors displayed activity only in the micromolar range.