2438-38-2

Usage

Uses

Used in Industrial Water Treatment:
Cyclohexanesulfonamide is used as a corrosion inhibitor in industrial water treatment processes. Its ability to prevent the corrosion of metal surfaces in contact with water makes it a valuable component in maintaining the integrity and longevity of industrial equipment and infrastructure.
Used in Plasticizer Industry:
Cyclohexanesulfonamide serves as a plasticizer, which is added to plastics to increase their flexibility, workability, and durability. Its use in this industry contributes to the production of a variety of plastic products with enhanced performance characteristics.
Used in Pharmaceutical Production:
Cyclohexanesulfonamide is utilized as an intermediate in the production of pharmaceuticals. Its role in the synthesis of various drugs highlights its importance in the development of new and effective medications for various medical conditions.
Used in Agrochemical Production:
In the agrochemical industry, Cyclohexanesulfonamide is employed as an intermediate in the synthesis of various agrochemicals. Its contribution to the development of crop protection products and other agricultural chemicals plays a crucial role in ensuring food security and sustainable agriculture.
However, it is important to note that Cyclohexanesulfonamide is toxic to aquatic organisms and may cause long-term adverse effects in the aquatic environment. It is also considered a mild irritant to the skin, eyes, and respiratory system. Therefore, proper handling, storage, and disposal practices should be followed to minimize potential harm to human health and the environment.

InChI:InChI=1/C6H13NO2S/c7-10(8,9)6-4-2-1-3-5-6/h6H,1-5H2,(H2,7,8,9)

Upstream product

• 2387-23-7 1,3-Dicyclohexylurea 
• 7664-41-7 ammonia 
• 4837-38-1 cyclohexanesulfonyl chloride 
• 1569-69-3 Cyclohexanethiol 
• 88304-20-5 isobutylidene-cyclohexylamine 

Downstream Products

• 1610042-45-9 N-(3-chloro-1,4-dioxo-1,4-dihydronaphthalen-2-yl)-cyclohexanesulfonamide 
• 1610042-54-0 N-(3-((3,5-dimethylphenyl)amino)-1,4-dioxo-1,4-dihydronaphthalen-2-yl)cyclohexanesulfonamide 
• 1609109-60-5 C₃₄H₄₈N₄O₅S 
• 90729-21-8 N-ethyl-N'-cyclohexanesulfonyl-urea 
• 3321-29-7 N-butyl-N'-cyclohexanesulfonyl-urea 
• 99066-09-8 cyclohexanesulfonyl-carbamic acid ethyl ester 
• 98428-73-0 cyclohexanesulfonyl-urea 
• 926299-66-3 N-(cyclohexylsulfonyl)-3-[1-(2,4-dichlorobenzyl)-3-isopropoxy-1H-pyrazol-5-yl]propanamide 

Relevant academic research and scientific papers

SELECTIVE NON-CYCLIC NUCLEOTIDE ACTIVATORS FOR THE CAMP SENSOR EPAC1

The invention relates generally to novel EPAC1 activators, such as Formula (I) and (II) and the preparation thereof as well as the use of EPAC1 activators disclosed herein as to selectively activate EPAC1 in cells.

NEW BRAF INHIBITORS AS PARADOX BREAKERS

The invention provides a novel compound having the general formula (I) (I) wherein R1-R3 and X are as defined in the description and in the claims. The compound of formula (I) can be used as a medicament.

Synthesis and Biochemical Evaluation of Noncyclic Nucleotide Exchange Proteins Directly Activated by cAMP 1 (EPAC1) Regulators

Exchange proteins directly activated by cAMP (EPAC) play a central role in various biological functions, and activation of the EPAC1 protein has shown potential benefits for the treatment of various human diseases. Herein, we report the synthesis and biochemical evaluation of a series of noncyclic nucleotide EPAC1 activators. Several potent EPAC1 binders were identified including 25g, 25q, 25n, 25u, 25e, and 25f, which promote EPAC1 guanine nucleotide exchange factor activity in vitro. These agonists can also activate EPAC1 protein in cells, where they exhibit excellent selectivity toward EPAC over protein kinase A and G protein-coupled receptors. Moreover, 25e, 25f, 25n, and 25u exhibited improved selectivity toward activation of EPAC1 over EPAC2 in cells. Of these, 25u was found to robustly inhibit IL-6-activated signal transducer and activator of transcription 3 (STAT3) and subsequent induction of the pro-inflammatory vascular cell adhesion molecule 1 (VCAM1) cell-adhesion protein. These novel EPAC1 activators may therefore act as useful pharmacological tools for elucidation of EPAC function and promising drug leads for the treatment of relevant human diseases.

Highly Chemoselective NH- and O-Transfer to Thiols Using Hypervalent Iodine Reagents: Synthesis of Sulfonimidates and Sulfonamides

Aryl thiols can be selectively converted to sulfonimidates or sulfonamides with three new S-X connections being made selectively in one pot. Using hypervalent iodine reagents in the presence of ammonium carbamate, NH- and O-groups are transferred under mild and practical conditions. Reducing the loading of ammonium carbamate changed the product distribution, converting the sulfonimidate to the sulfonamide. Studies into the possible intermediate species are presented, suggesting that multiple pathways may be possible via sulfinate esters, or related intermediates, with each species forming the same products.

THIAZOLIDINONE COMPOUNDS AND USE THEREOF

A pharmaceutical composition containing a compound of Formula (I) for treating an opioid receptor-associated condition. Also disclosed is a method for treating an opioid receptor-associated condition using such a compound. Further disclosed are two sets of thiazolidinone compounds of formula (I): (i) compounds each having an enantiomeric excess greater than 90% and (ii) compounds each being substituted with deuterium.

SULFONYLUREAS AND RELATED COMPOUNDS AND USE OF SAME

ABSTRACT The present invention provides for certain sulfonyl ureas and related compounds which have advantageous properties and show useful activity in the inhibition of activation of the NLRP3 inflammasome. Such compounds are useful in the treatment of a wide range of disorders in which the inflammation process, or more specifically the NLRP3 inflammasome, have been implicated as being a key factor.

A general iodine-mediated synthesis of primary sulfonamides from thiols and aqueous ammonia

A general and efficient methodology for preparing primary sulfonamides has been developed. In the presence of iodine as the catalyst and TBHP (70% in water) as the oxidant, a wide range of primary sulfonamides were prepared from the corresponding thiols and aqueous ammonia in moderate to good yields.

Structure-activity relationships and colorimetric properties of specific probes for the putative cancer biomarker human arylamine N-acetyltransferase 1

A naphthoquinone inhibitor of human arylamine N-acetyltransferase 1 (hNAT1), a potential cancer biomarker and therapeutic target, has been reported which undergoes a distinctive concomitant color change from red to blue upon binding to the enzyme. Here we describe the use of in silico modeling alongside structure-activity relationship studies to advance the hit compound towards a potential probe to quantify hNAT1 levels in tissues. Derivatives with both a fifty-fold higher potency against hNAT1 and a two-fold greater absorption coefficient compared to the initial hit have been synthesized; these compounds retain specificity for hNAT1 and its murine homologue mNat2 over the isoenzyme hNAT2. A relationship between pKa, inhibitor potency and colorimetric properties has also been uncovered. The high potency of representative examples against hNAT1 in ZR-75-1 cell extracts also paves the way for the development of inhibitors with improved intrinsic sensitivity which could enable detection of hNAT1 in tissue samples and potentially act as tools for elucidating the unknown role hNAT1 plays in ER+ breast cancer; this could in turn lead to a therapeutic use for such inhibitors.

Identification of the first potent, selective and bioavailable PPARα antagonist

The discovery and SAR of a novel series of potent and selective PPARα antagonists are herein described. Exploration of replacements for the labile acyl sulfonamide linker led to a biaryl sulfonamide series of which compound 33 proved to be suitable for further profiling in vivo. Compound 33 demonstrated excellent potency, selectivity against other nuclear hormone receptors, and good pharmacokinetics in mouse.

Hepatitis C Virus Inhibitors

Hepatitis C virus inhibitors having the general formula are disclosed. Compositions comprising the compounds and methods for using the compounds to inhibit HCV are also disclosed.