180977-04-2

Basic information

• Product Name: (S)-2-{[5-((R)-2-tert-Butoxycarbonylamino-3-tritylsulfanyl-propionylamino)-biphenyl-2-carbonyl]-amino}-4-methylsulfanyl-butyric acid methyl ester
• CAS NO: 180977-04-2
• Molecular Weight: 804.044
• Mol File: 180977-04-2.mol

Chemical Properties

• CAS DataBase Reference: (S)-2-{[5-((R)-2-tert-Butoxycarbonylamino-3-tritylsulfanyl-propionylamino)-biphenyl-2-carbonyl]-amino}-4-methylsulfanyl-butyric acid methyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: (S)-2-{[5-((R)-2-tert-Butoxycarbonylamino-3-tritylsulfanyl-propionylamino)-biphenyl-2-carbonyl]-amino}-4-methylsulfanyl-butyric acid methyl ester(180977-04-2)
• EPA Substance Registry System: (S)-2-{[5-((R)-2-tert-Butoxycarbonylamino-3-tritylsulfanyl-propionylamino)-biphenyl-2-carbonyl]-amino}-4-methylsulfanyl-butyric acid methyl ester(180977-04-2)

Safety Data

• Hazardous Substances Data: 180977-04-2(Hazardous Substances Data)

Upstream product

• 180977-03-1 4-amino-2-phenylbenzoylmethionine methyl ester 
• 7745-93-9 2-bromo-4-nitrotoluene 
• 13480-38-1 4-Nitro-2-phenyltoluene 
• 21947-98-8 N-tert-butyloxycarbonyl-S-trityl-L-cysteine 
• 180977-02-0 N-[4-nitro-2-phenylbenzoyl]-methionine methyl ester 
• 98-80-6 phenylboronic acid 

Relevant articles and documents

Probing the hydrophobic pocket of farnesyltransferase: Aromatic substitution of CAAX peptidomimetics leads to highly potent inhibitors

Cysteine farnesylation at the carboxylate terminal tetrapeptide CAAX of Ras protein is catalyzed by farnesyltransferase. This lipid modification is necessary for regulatory function of both normal and oncogenic Ras. The high frequency of Ras mutation in human cancers has prompted an intensive study on finding ways of controlling oncogenic Ras function. Inhibition of farnesyltransferase is among the most sought after targets for cancer chemotherapy. We report here the design, synthesis and biological characterization of a series of peptidomimetics as farnesyltransferase inhibitors. These compounds are extremely potent towards farnesyltransferase with IC50 values ranging from subnanomolar to low nanomolar concentrations. They have a high selectivity for farnesyltransferase over the closely related geranylgeranyltransferase-I. Structure-activity relationship studies demonstrated that a properly positioned hydrophobic group significantly enhanced inhibition potency, reflecting an improved complementarity to the large hydrophobic pocket in the CAAX binding site. Copyright (C) 1999 Elsevier Science Ltd.