853771-88-7

Usage

Uses

Used in Pharmaceutical Industry:
4-BROMO-2-(TRIFLUOROMETHOXY)ANISOLE is used as a biological evaluation agent for the development of novel antitumor drugs. Its unique structure and potential biological activity make it a promising candidate for further research and development in the field of oncology.
In the context of biological evaluation, 4-BROMO-2-(TRIFLUOROMETHOXY)ANISOLE is employed to assess its potential as an analog of existing antitumor agents. This involves testing its efficacy, safety, and mechanism of action in various in vitro and in vivo models to determine its suitability as a therapeutic agent for cancer treatment.

InChI:InChI=1/C8H6BrF3O2/c1-13-6-3-2-5(9)4-7(6)14-8(10,11)12/h2-4H,1H3

Upstream product

• 690264-39-2 4-bromo-2-(trifluoromethoxy)phenol 
• 74-88-4 methyl iodide 
• 32858-93-8 2-(trifluoromethoxy)phenol 

Downstream Products

• 647855-22-9 4-methoxy-3-(trifluoromethoxy)-benzoic acid 

Relevant academic research and scientific papers

CYANOCYCLOPROPYLCARBOXAMIDES AS CATHEPSIN INHIBITORS

The present invention relates to compounds of formula (I) for treating diseases associated with cysteine protease activity. The compounds are reversible inhibitors of cysteine proteases, including cathepsins B, K, C, F, H, L, O, S, W and X. Of particular interest are diseases associated with Cathepsin K.

Potent, novel in vitro inhibitors of the Pseudomonas aeruginosa deacetylase LpxC

Deacetylation of uridyldiphospho-3-O-(R-hydroxydecanoyl)-N-acetylglucosamine by LpxC is the first committed step in the Pseudomonas aeruginosa biosynthetic pathway to lipid A; homologous enzymes are found widely among Gram-negative bacteria. As an essential enzyme for which no inhibitors have yet been reported, the P. aeruginosa LpxC represents a highly attractive target for a novel antibacterial drug. We synthesized several focused small-molecule libraries, each composed of a variable aromatic ring, one of four heterocyclic/spacer moieties, and a hydroxamic acid and evaluated the LpxC inhibition of these compounds against purified P. aeruginosa enzyme. To ensure that the in vitro assay would be as physiologically relevant as possible, we synthesized a tritiated form of the specific P. aeruginosa glycolipid substrate and measured directly the enzymatically released acetate. Several of our novel compounds, predominantly those having fluorinated substituents on the aromatic ring and an oxazoline as the heterocyclic moiety, demonstrated in vitro IC50 values less than 1 μM. We now report the synthesis and in vitro evaluation of these P. aeruginosa LpxC inhibitors.