201669-82-1

Basic information

• Product Name: {(R)-1-[(3'-Methyl-biphenyl-4-ylamino)-methyl]-2-tritylsulfanyl-ethyl}-carbamic acid tert-butyl ester
• Synonyms: {(R)-1-[(3'-Methyl-biphenyl-4-ylamino)-methyl]-2-tritylsulfanyl-ethyl}-carbamic acid tert-butyl ester
• CAS NO: 201669-82-1
• Molecular Weight: 614.852
• Mol File: 201669-82-1.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: {(R)-1-[(3'-Methyl-biphenyl-4-ylamino)-methyl]-2-tritylsulfanyl-ethyl}-carbamic acid tert-butyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: {(R)-1-[(3'-Methyl-biphenyl-4-ylamino)-methyl]-2-tritylsulfanyl-ethyl}-carbamic acid tert-butyl ester(201669-82-1)
• EPA Substance Registry System: {(R)-1-[(3'-Methyl-biphenyl-4-ylamino)-methyl]-2-tritylsulfanyl-ethyl}-carbamic acid tert-butyl ester(201669-82-1)

Safety Data

• Hazardous Substances Data: 201669-82-1(Hazardous Substances Data)

Upstream product

• 21947-98-8 N-tert-butyloxycarbonyl-S-trityl-L-cysteine 
• 952-21-6 4-nitro-3'-methylbiphenyl 
• 17933-03-8 m-tolylboronic acid 
• 586-78-7 para-nitrophenyl bromide 
• 158861-38-2 (R)-N-methyl-N-methoxy-2-tert-butoxycarbonylamino-3-(triphenylmethylthio)propionamide 

Relevant articles and documents

Design and synthesis of non-peptide Ras CAAX mimetics as potent farnesyltransferase inhibitors

Cysteine farnesylation of the ras oncogene product Ras is required for its transforming activity and is catalyzed by farnesyltransferase (FTase). The Ras carboxyl terminal tetrapeptide CAAX (C is cysteine, A is any aliphatic amino acid, X is methionine or serine) is the minimum sequence for FTase recognition. We report here the design, synthesis, and biological characterization of Ras CAAX non-peptide mimetics in which the cysteine is linked through a reduced pseudopeptide bond to 4-amino-3'-carboxybiphenyl. These non-peptide mimetics are potent inhibitors of FTase (IC50 = 40 nM for the most potent inhibitor) and are highly selective for FTase over GGTase I (geranylgeranyltransferase I). They are not substrates for farnesylation, do not have peptidic features, and have no hydrolyzable bonds. Structure- activity studies reveal the importance of the position of the carboxylic acid on the aryl ring as well as the reduction of the cysteine amide bond. Substitution at the 2-position of 4-amino-3'-carboxybiphenyl increases inhibitory potency, while the removal of the carboxylic acid results in a 10- fold loss of inhibitory activity.