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Usage

Uses

Used in Organic Synthesis:
3-(4-Methanesulfonylphenyl)benzoic acid is used as a building block in organic synthesis for the creation of various pharmaceuticals and agrochemicals, contributing to the development of new and effective chemical compounds.
Used in Medicinal Chemistry:
In the field of medicinal chemistry, 3-(4-Methanesulfonylphenyl)benzoic acid serves as a key intermediate, aiding in the synthesis of pharmaceuticals that address a range of health conditions.
Used in Dye and Pigment Production:
3-(4-Methanesulfonylphenyl)benzoic acid is utilized as a crucial intermediate in the production of dyes and pigments, enhancing the color properties and performance of these compounds in various applications.
Overall, 3-(4-Methanesulfonylphenyl)benzoic acid is a versatile compound with applications across multiple industries, including pharmaceuticals, agrochemicals, and dye and pigment manufacturing.

Upstream product

• 104-95-0 (4-bromophenyl)thioanisole 
• 585-76-2 m-bromobenzoic acid 
• 149104-88-1 4-methanesulphonylphenylboronic acid 
• 106-53-6 para-bromobenzenethiol 
• 3466-32-8 4-bromoohenyl methyl sulfone 
• 25487-66-5 3-Carboxyphenylboronic 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 Small-Molecule Inhibitors of the ATPase Activity of Human Papillomavirus E1 Helicase

The Boehringer Ingelheim compound collection was screened for inhibitors of the ATPase activity of human papillomavirus E1 helicase to develop antiviral agents that inhibit human papillomavirus (HPV) DNA replication. This screen led to the discovery of (biphenyl-4-sulfonyl)acetic acid 1, which inhibits the ATPase activity of HPV type 6 E1 helicase with a low micromolar IC50 value. A hit-to-lead exercise rapidly converted 1 into a low nanomolar lead series.