1494-85-5

Usage

Uses

Used in Pharmaceutical Industry:
Celecoxib is used as an analgesic and anti-inflammatory agent for the treatment of various conditions characterized by pain and inflammation. Its primary applications include the management of osteoarthritis, rheumatoid arthritis, and ankylosing spondylitis, where it helps to reduce the symptoms and improve the quality of life for patients.
Used in Pain Management:
Celecoxib serves as a pain reliever, particularly for those suffering from chronic conditions that involve inflammation. By inhibiting COX-2, it effectively reduces the levels of prostaglandins, which are responsible for pain sensation, thus providing relief to patients.
Used in Inflammation Control:
In conditions where inflammation is a significant factor, celecoxib is utilized to control the inflammatory response. Its ability to inhibit prostaglandin production helps in reducing the inflammation associated with various diseases and injuries.
Used in Oncology:
Research has shown that celecoxib, due to its COX-2 inhibitory properties, may also have potential applications in oncology. It is being studied for its possible role in reducing the risk of certain types of cancer, particularly those associated with chronic inflammation, and for its potential synergistic effects when used in combination with other cancer treatments.
Used in Veterinary Medicine:
Celecoxib is also used in veterinary medicine for the treatment of pain and inflammation in animals, similar to its applications in human medicine. It provides a valuable option for managing conditions like arthritis in pets, improving their mobility and comfort.

InChI:InChI=1/C12H11FN2O2S/c13-9-1-5-11(6-2-9)15-18(16,17)12-7-3-10(14)4-8-12/h1-8,15H,14H2

Upstream product

• 121-60-8 p-acetylaminobenzenesulfonyl chloride 
• 98-74-8 4-Nitrobenzenesulfonyl chloride 
• 103-84-4 Acetanilid 
• 371-40-4 4-fluoroaniline 
• 1545-96-6 N-(4-fluorophenyl)-4-nitrobenzene sulphonamide 
• 599-78-0 N-(4-(N-(4-fluorophenyl)sulfamoyl)phenyl)acetamide 

Downstream Products

• 1398023-32-9 C₂₁H₁₇FN₂O₅S 
• 349470-56-0 N-(4-fluorophenyl)-4-(phenylureido)benzene sulphonamide 
• 1160212-25-8 C₁₉H₁₅FN₂O₆S 
• 1023311-07-0 N-(4-fluorophenyl)-4-isothiocyanato-benzenesulfonamide 
• 383-43-7 N-[4-(4-fluoro-phenylsulfamoyl)-phenyl]-succinamic acid 
• 387-28-0 N,N-succinyl-sulfanilic acid-(4-fluoro-anilide) 

Relevant academic research and scientific papers

Comparative study between the anti-P. falciparum activity of triazolopyrimidine, pyrazolopyrimidine and quinoline derivatives and the identification of new PfDHODH inhibitors

In this work, we designed and synthesized 35 new triazolopyrimidine, pyrazolopyrimidine and quinoline derivatives as P. falciparum inhibitors (3D7 strain). Thirty compounds exhibited anti-P. falciparum activity, with IC50 values ranging from 0.030 to 9.1 μM. The [1,2,4]triazolo[1,5-a]pyrimidine derivatives were more potent than the pyrazolo[1,5-a]pyrimidine and quinoline analogues. Compounds 20, 21, 23 and 24 were the most potent inhibitors, with IC50 values in the range of 0.030–0.086 μM and were equipotent to chloroquine. In addition, the compounds were selective, showing no cytotoxic activity against the human hepatoma cell line HepG2. All [1,2,4]triazolo[1,5-a]pyrimidine derivatives inhibited PfDHODH activity in the low micromolar to low nanomolar range (IC50 values of 0.08–1.3 μM) and did not show significant inhibition against the HsDHODH homologue (0–30% at 50 μM). Molecular docking studies indicated the binding mode of [1,2,4]triazolo[1,5-a]pyrimidine derivatives to PfDHODH, and the highest interaction affinities for the PfDHODH enzyme were in agreement with the in vitro experimental evaluation. Thus, the most active compounds against P. falciparum parasites 20 (R = CF3, R1 = F; IC50 = 0.086 μM), 21 (R = CF3; R1 = CH3; IC50 = 0.032 μM), 23, (R = CF3, R1 = CF3; IC50 = 0.030 μM) and 24 (R = CF3, 2-naphthyl; IC50 = 0.050 μM) and the most active inhibitor against PfDHODH 19 (R = CF3, R1 = Cl; IC50 = 0.08 μM - PfDHODH) stood out as new lead compounds for antimalarial drug discovery. Their potent in vitro activity against P. falciparum and the selective inhibition of the PfDHODH enzyme strongly suggest that this is the mechanism of action underlying this series of new [1,2,4]triazolo[1,5-a]pyrimidine derivatives.

Sulphonamidic Groups as Electron-Withdrawing Units in Ureido-Based Anion Receptors: Enhanced Anion Complexation versus Deprotonation

A sulphonamidic moiety was utilized as an electron-withdrawing group for enhancement of anion complexation features of urea-based receptors. A series of receptors varying in acidity of sulphonamidic and urea NH groups was synthesized and thoroughly tested. The individual complexation properties reflect deprotonation/complexation equilibrium in a given molecule as a function of the substitution. The receptors containing electron-donating groups in conjugation to the sulphonamidic moiety showed higher association constants towards H2PO4? and carboxylate anions, while those containing electron-withdrawing groups inclined to deprotonation of sulphonamidic NH. The deprotonation issue can be avoided by alkylation at the early step of receptor synthesis or it can be utilized for insertion of suitable groups that enable its anchoring on various substrates to form more elaborated receptor structures.

Synthesis, characterization, crystal structures and biological screening of 4-amino quinazoline sulfonamide derivatives

Three quinazolin-4-ylamino derivatives containing phenylbenzenesulfonamides (7a-7c)were synthesized by reacting (E)-N'-(2-cyanophenyl)-N,N-dimethyl formamidine (6)with different 4-amino-N-(phenyl)benzenesulfonamides (4a-4c)and characterized by different techniques such as HRMS, IR, 1H NMR and 13C NMR spectroscopy. The structural properties were further examined by single crystal X-ray diffraction method. The X-ray data shows that compounds 7a and 7c contain two molecules and 7b contains one molecule in the asymmetric unit. Comparison of conformation of two distinct molecules, “A” and “B”, in the asymmetric unit of 7a and 7c were studied with the aid of reported literature. The in vitro antiproliferative activity of the compounds was tested against two breast cancer cell lines (MDA-MB-231 and MCF7). Compound 7b observed as a highest potent candidate against MDA-MB-231with IC50 of 5.44 μg/mL. Antimicrobial activity was also screened against bacterial and fungal strains. Compound 7a with chloro substitution was observed as the most potent candidate against the Gram-negative bacterial strains, whereas the compounds showed no significant activity against the fungal strain.

Benzsulfamide IDO1 inhibitor, and preparation method and application thereof

The invention belongs to the field of drugs, and particularly relates to a benzsulfamide compound having a structural characteristic as shown in formula (I) or pharmaceutically acceptable salt of the benzsulfamide compound, a preparation method of the benzsulfamide compound or the salt, and uses of the benzsulfamide compound or the salt as an indoleamine 2,3-dioxygenase 1 (IDO1) inhibitor. An experimental result indicates that the compound provided by the invention has an obvious inhibiting effect on the activity of the IDO1, can effectively promote T cell proliferation, inhibits native T cells from differentiating into regulatory T cells, reverses immunosuppression mediated by the IDO1, and can be used for treating relevant diseases having pathological characteristics of metabolic pathways of kynurenine mediated by the IDO1, including cancer, virus infection, neurodegenerative diseases, cataract, organ transplant rejection, depression, autoimmune diseases and the like. Formula (I) is shown in the description.

Design, synthesis, and evaluation of substituted nicotinamide adenine dinucleotide (NAD+) synthetase inhibitors as potential antitubercular agents

Nicotinamide adenine dinucleotide (NAD+) synthetase catalyzes the last step in NAD+ biosynthesis. Depletion of NAD+ is bactericidal for both active and dormant Mycobacterium tuberculosis (Mtb). By inhibiting NAD+ synthetase (NadE) from Mtb, we expect to eliminate NAD+ production which will result in cell death in both growing and nonreplicating Mtb. NadE inhibitors have been investigated against various pathogens, but few have been tested against Mtb. Here, we report on the expansion of a series of urea-sulfonamides, previously reported by Brouillette et al. Guided by docking studies, substituents on a terminal phenyl ring were varied to understand the structure–activity-relationships of substituents on this position. Compounds were tested as inhibitors of both recombinant Mtb NadE and Mtb whole cells. While the parent compound displayed very weak inhibition against Mtb NadE (IC50 = 1000 μM), we observed up to a 10-fold enhancement in potency after optimization. Replacement of the 3,4-dichloro group on the phenyl ring of the parent compound with 4-nitro yielded 4f, the most potent compound of the series with an IC50 value of 90 μM against Mtb NadE. Our modeling results show that these urea-sulfonamides potentially bind to the intramolecular ammonia tunnel, which transports ammonia from the glutaminase domain to the active site of the enzyme. This hypothesis is supported by data showing that, even when treated with potent inhibitors, NadE catalysis is restored when treated with exogenous ammonia. Most of these compounds also inhibited Mtb cell growth with MIC values of 19–100 μg/mL. These results improve our understanding of the SAR of the urea-sulfonamides, their mechanism of binding to the enzyme, and of Mtb NadE as a potential antitubercular drug target.

N-Acylated derivatives of sulfamethoxazole and sulfafurazole inhibit intracellular growth of chlamydia trachomatis

Antibacterial compounds with novel modes of action are needed for management of bacterial infections. Here we describe a high-content screen of 9,800 compounds identifying acylated sulfonamides as novel growth inhibitors of the sexually transmitted pathogen Chlamydia trachomatis. The effect was bactericidal and distinct from that of sulfonamide antibiotics, as para-Aminobenzoic acid did not reduce efficacy. Chemical inhibitors play an important role in Chlamydia research as probes of potential targets and as drug development starting points. Copyright

Structure-guided design of potent diazobenzene inhibitors for the BET bromodomains

BRD4, characterized by two acetyl-lysine binding bromodomains and an extra-terminal (ET) domain, is a key chromatin organizer that directs gene activation in chromatin through transcription factor recruitment, enhancer assembly, and pause release of the RNA polymerase II complex for transcription elongation. BRD4 has been recently validated as a new epigenetic drug target for cancer and inflammation. Our current knowledge of the functional differences of the two bromodomains of BRD4, however, is limited and is hindered by the lack of selective inhibitors. Here, we report our structure-guided development of diazobenzene-based small-molecule inhibitors for the BRD4 bromodomains that have over 90% sequence identity at the acetyl-lysine binding site. Our lead compound, MS436, through a set of water-mediated interactions, exhibits low nanomolar affinity (estimated Ki of 30-50 nM), with preference for the first bromodomain over the second. We demonstrated that MS436 effectively inhibits BRD4 activity in NF-κB-directed production of nitric oxide and proinflammatory cytokine interleukin-6 in murine macrophages. MS436 represents a new class of bromodomain inhibitors and will facilitate further investigation of the biological functions of the two bromodomains of BRD4 in gene expression.

Nitrogen-containing polyhydroxylated aromatics as HIV-1 integrase inhibitors: Synthesis, structure-activity relationship analysis, and biological activity

Four series of forty-five nitrogen-containing polyhydroxylated aromatics based on caffeic acid phenethyl ester were designed and synthesized as HIV-1 integrase (IN) inhibitors. Most of these compounds inhibited IN catalytic activities in low micromolar range. Among these new analogues, compounds 9e and 9f were the most potent IN inhibitors with IC50 value of 0.7 μM against strand transfer reaction. Their key structure-activity relationships were also discussed.

Design and synthesis of novel nitrogen-containing polyhydroxylated aromatics as HIV-1 integrase inhibitors from caffeic acid phenethyl ester

A series of nitrogen-containing polyhydroxylated aromatics from caffeic acid phenethyl ester were designed and synthesized as HIV-1 integrase inhibitors. Most of these compounds exhibited potent inhibitory activities at micromolar concentrations against HIV-1 integrase in the 3′-end processing and the strand transfer. Their key structure-activity relationship was also discussed.