180976-94-7

Usage

Uses

Used in Pharmaceutical Research:
BOC-4-AMINO-3-METHYLBENZOIC ACID is used as a key intermediate in the synthesis of various pharmaceuticals for its ability to protect the amine group during the synthesis process. This protection is crucial for the successful formation of desired peptide bonds and the development of new drugs with specific therapeutic properties.
Used in Organic Synthesis:
In the field of organic synthesis, BOC-4-AMINO-3-METHYLBENZOIC ACID serves as a versatile building block. It is utilized for the construction of a wide range of chemical compounds, contributing to the development of new materials and chemical entities with potential applications across various industries.
Used in Medicinal Chemistry:
BOC-4-AMINO-3-METHYLBENZOIC ACID is employed as a component in the design of biologically active molecules. Its presence in these molecules can influence their interaction with biological targets, making it an essential tool in the creation of new therapeutic agents and probes for biological research.
Used in Chemical Production:
BOC-4-AMINO-3-METHYLBENZOIC ACID is also used as a precursor in the production of various chemicals. Its versatility and reactivity make it a valuable component in the synthesis of specialty chemicals used in different applications, such as agrochemicals, dyes, and other industrial chemicals.

Upstream product

• 24424-99-5 di-tert-butyl dicarbonate 
• 2486-70-6 4-amino 3-methylbenzoic acid 

Downstream Products

• 180976-95-8 N-Boc-4-amino-3-methylbenzoyl methionine methyl ester 
• 1613027-08-9 tert-butyl (6-methyl-1,3-dioxo-2-phenylisoindolin-5-yl)carbamate 
• 180976-97-0 (S)-2-[4-((R)-2-tert-Butoxycarbonylamino-3-tritylsulfanyl-propionylamino)-3-methyl-benzoylamino]-4-methylsulfanyl-butyric acid methyl ester 

Relevant academic research and scientific papers

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.

Inhibitors of prenyl transferases

Compounds which inhibit prenyl transferases, particularly farnysyltransferase and geranylgeranyl transferase I, processes for preparing the compounds, pharmaceutical compositions containing the compounds, and methods of use.

Inhibitors of farnesyltransferase

Peptidomimetics of the formula CβX where C is cysteine, X is any naturally occuring amino acid, and β is a hydrophobic spacer, most notably 2-phenyl-4-aminobenzoic acid. These compounds are effective inhibitors of p2lras farnesyltrasferase, block Ras-dependent oncogenic signalling and inhibit human tumor growth in vivo in animal models. Pro-drugs made by functionalizing terminal amino and carboxylic acid groups of peptides and peptidomimetics are also disclosed. Such functionalized derivatives demonstrate increased cell uptake. Other structural modifications are also disclosed.