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Usage

Uses

Used in Pharmaceutical Industry:
4'-Acetyl-biphenyl-3-carboxylic acid is used as an intermediate in the synthesis of pharmaceuticals for its potential anti-inflammatory and analgesic properties. It is particularly valuable in the development of new anti-inflammatory agents due to its potential as a selective cyclooxygenase-2 (COX-2) inhibitor.
Used in Agrochemical Industry:
In the agrochemical industry, 4'-acetyl-biphenyl-3-carboxylic acid is utilized as a building block in the creation of various agrochemicals, contributing to the development of effective products for agricultural applications.
Used in Research and Development:
4'-Acetyl-biphenyl-3-carboxylic acid serves as a key compound in research and development initiatives, particularly in the exploration of its potential as a selective COX-2 inhibitor. This makes it instrumental in the advancement of novel anti-inflammatory therapies and the study of its underlying mechanisms of action.

Upstream product

• 25487-66-5 3-Carboxyphenylboronic acid 
• 99-90-1 para-bromoacetophenone 
• 585-76-2 m-bromobenzoic acid 
• 149104-90-5 4-acetylphenylboronic acid 

Relevant academic research and scientific papers

A focused fragment library targeting the antibiotic resistance enzyme - Oxacillinase-48: Synthesis, structural evaluation and inhibitor design

β-Lactam antibiotics are of utmost importance when treating bacterial infections in the medical community. However, currently their utility is threatened by the emergence and spread of β-lactam resistance. The most prevalent resistance mechanism to β-lactam antibiotics is expression of β-lactamase enzymes. One way to overcome resistance caused by β-lactamases, is the development of β-lactamase inhibitors and today several β-lactamase inhibitors e.g. avibactam, are approved in the clinic. Our focus is the oxacillinase-48 (OXA-48), an enzyme reported to spread rapidly across the world and commonly identified in Escherichia coli and Klebsiella pneumoniae. To guide inhibitor design, we used diversely substituted 3-aryl and 3-heteroaryl benzoic acids to probe the active site of OXA-48 for useful enzyme-inhibitor interactions. In the presented study, a focused fragment library containing 49 3-substituted benzoic acid derivatives were synthesised and biochemically characterized. Based on crystallographic data from 33 fragment-enzyme complexes, the fragments could be classified into R1 or R2 binders by their overall binding conformation in relation to the binding of the R1 and R2 side groups of imipenem. Moreover, binding interactions attractive for future inhibitor design were found and their usefulness explored by the rational design and evaluation of merged inhibitors from orthogonally binding fragments. The best inhibitors among the resulting 3,5-disubstituted benzoic acids showed inhibitory potential in the low micromolar range (IC50 = 2.9 μM). For these inhibitors, the complex X-ray structures revealed non-covalent binding to Arg250, Arg214 and Tyr211 in the active site and the interactions observed with the mono-substituted fragments were also identified in the merged structures.

Discovery of a potent and selective series of pyrazole bacterial methionyl-tRNA synthetase inhibitors

Starting with a micromolar lead identified from high-throughput screening, a series of pyrazoles were discovered with significantly improved potency on bacterial methionyl-tRNA synthetase and selectivity over human methionyl-tRNA synthetase.