3609-50-5

Usage

Uses

4-(1-Hydroxy-1-methylethyl)benzoic Acid is a cuminaldehyde derivative

InChI:InChI=1/C10H12O3/c1-10(2,13)8-5-3-7(4-6-8)9(11)12/h3-6,13H,1-2H3,(H,11,12)

Upstream product

• 536-66-3 p-isopropylbenzoic acid 
• 13816-33-6 p-Cyanocumen 
• 536-60-7 cuminol 
• 1830-69-9 4-(prop-1-en-2-yl)benzoic acid 
• 99-87-6 4-methylisopropylbenzene 
• 7732-18-5 water 
• 7664-93-9 sulfuric acid 
• 6712-78-3 myrtenol 
• 619-58-9 4-iodobenzoic acid 
• 67-64-1 acetone 
• 64-18-6 formic acid 

Downstream Products

• 536-66-3 p-isopropylbenzoic acid 
• 1830-69-9 4-(prop-1-en-2-yl)benzoic acid 
• 26581-23-7 4-(1-methylethenyl)benzoic acid methyl ester 
• 3609-53-8 methyl 4-acetylbenzoate 
• 50604-11-0 4-(1-methoxy-1-methylethyl)benzoic acid 
• 50604-10-9 methyl 4-(1-methoxy-1-methylethyl)benzoate 
• 50604-12-1 methyl p-(1-hydroxy-1-methylethyl)benzoate 

Relevant academic research and scientific papers

Discovery of N-phenyl-1-(phenylsulfonamido)cyclopropane-1-carboxamide analogs as NLRP3 inflammasome inhibitors

Two series of novel NLRP3 inflammasome inhibitors are designed, synthesized, and evaluated in an effort to develop diversified analogs based on the N-(phenylcarbamoyl)benzenesulfonamide scaffold. SAR studies reveal that the sulfonylurea linker can tolerate chemical modifications with either simply changing over the position of carbonyl and sulfonyl group or structurally flexibly inserting a cyclopropyl group, leading to identification of several more potent and diversified NLRP3 antagonists (e.g., 9) with low nanomolar inhibitory activities. Further studies indicate that these two series of compounds with low cytotoxicity exhibited weak effects on the generation of NO and TNF-a. The findings may serve as good starting points for the development of more potent NLRP3 inflammasome inhibitors as valuable pharmacological probes or potential drug candidates.

Stepwise benzylic oxygenation via uranyl-photocatalysis

Stepwise oxygenation at the benzylic position (1°, 2°, 3°) of aromatic molecules was comprehensively established under ambient conditions via uranyl photocatalysis to produce carboxylic acids, ketones, and alcohols, respectively. The accuracy of the stepwise oxygenation was ensured by the tunability of catalytic activity in uranyl photocatalysis, which was adjusted by solvents and additives demonstrated through Stern–Volmer analysis. Hydrogen atom transfer between the benzylic position and the uranyl catalyst facilitated oxygenation, further confirmed by kinetic studies. Considerably improved efficiency of flow operation demonstrated the potential for industrial synthetic application.

Second-Generation Dual FXR/sEH Modulators with Optimized Pharmacokinetics

Non-alcoholic steatohepatitis (NASH) presents as an epidemic chronic liver disease that is closely associated with metabolic disorders and involves hepatic steatosis, inflammation, and fibrosis as key factors. Despite the enormous global prevalence of NASH, effective pharmacological interventions are lacking. Based on the hypothesis that the multifactorial condition NASH may benefit from combined multiple modes of action for enhanced therapeutic efficacy, we have previously developed dual FXR activators/sEH inhibitors (FXRa/sEHi) and observed remarkable antifibrotic effects upon their use in rodent NASH models. However, these first-generation FXRa/sEHi were characterized by moderate metabolic stability and short in vivo half-life. Aiming to overcome these pharmacokinetic drawbacks, we have systematically studied the structure-activity and structure-stability relationships of the chemotype and obtained second-generation FXRa/sEHi with improved pharmacokinetic parameters. With high plasma exposure, a half-life greater than 5 h, and similar dual potency on the intended targets, 13 presents as a substantially optimized FXRa/sEHi for late-stage preclinical development.

NLRP3 inflammasome inhibitor and preparation method and application thereof

The invention relates to a class of 1, 2, 3, 5, 6, 7 hexahydrosymmetric indacene compounds containing one or more substituents., pharmaceutically acceptable salts, esters or hydrates thereof, a preparation method thereof, a pharmaceutical composition containing the compounds, and an application of the compounds as a novel NLRP3 inflammasome inhibitor in preparation of drugs for preventing and/or treating diseases related to NLRP3 inflammasome.

Method for selectively oxidizing cumene compounds

The invention relates to a method for selectively oxidizing cumene compounds, and the method comprises the following steps: placing cumene compounds shown in a formula (I), an iron porphyrin catalyst,an oxidant and a dispersant into a ball milling tank, sealing the ball milling tank, performing ball milling for 3 to 24 hours at a rotating speed of 100 to 800 rpm at room temperature, stopping ballmilling once every 1 to 3 hours in the ball milling process, discharging gases in the ball milling tank, finishing the reaction, and performing post-treatment on a reaction mixture to obtain product2-phenyl-2-propanol compound shown in a formula (II); according to the invention, the oxidation conversion of the cumene and derivatives thereof is realized through solid-phase ball milling, the reaction mode is novel, the operation is convenient, and the energy consumption is low; the method needs no organic solvent, thus effectively avoiding the use of toxic and harmful organic solvents and being green and environment-friendly; has low peroxide content and high safety factor, and high 2-phenyl-2-propanol and derivative selectivity and meets the social requirements of the current green chemical process, environmental compatibility chemical process and biological compatibility chemical process.

PYRAZOLO[3,4-b]PYRIDINE AND PYRROLO[2,3-b]PYRIDINE INHIBITORS OF BRUTON'S TYROSINE KINASE

Disclosed are pyrazolo[3,4-b]pyridine and pyrrolo[2,3-b]pyridine inhibitors of Bruton's tyrosine kinase (Btk). Also disclosed are pharmaceutical compositions that include the compounds. Methods of using the Btk inhibitors are described, alone or in combin

MODULATORS OF METHYL MODIFYING ENZYMES, COMPOSITIONS AND USES THEREOF

Agents for modulating methyl modifying enzymes, compositions and uses thereof are provided herein.

INHIBITORS OF BRUTON'S TYROSINE KINASE

This application discloses compounds according to generic Formula I: wherein all variables are defined as described herein, which inhibit Btk. The compounds disclosed herein are useful to modulate the activity of Btk and treat diseases associated with exc

MODULATORS OF METHYL MODIFYING ENZYMES, COMPOSITIONS AND USES THEREOF

Agents for modulating methyl modifying enzymes, compositions and uses thereof are provided herein.

Investigation of the substrate range of CYP199A4: Modification of the partition between hydroxylation and desaturation activities by substrate and protein engineering

The cytochrome P450 enzyme CYP199A4, from Rhodopseudomonas palustris HaA2, can efficiently demethylate 4-methoxybenzoic acid. It is also capable of oxidising a range of other related substrates. By investigating substrates with different substituents and ring systems we have been able to show that the carboxylate group and the nature of the ring system and the substituent are all important for optimal substrate binding and activity. The structures of the veratric acid, 2-naphthoic acid and indole-6-carboxylic acid substrate-bound CYP199A4 complexes reveal the substrate binding modes and the side-chain conformational changes of the active site residues to accommodate these larger substrates. They also provide a rationale for the selectivity of product oxidation. The oxidation of alkyl substituted benzoic acids by CYP199A4 is more complex, with desaturation reactions competing with hydroxylation activity. The structure of 4-ethylbenzoic acid-bound CYP199A4 revealed that the substrate is held in a similar position to 4-methoxybenzoic acid, and that the C β C-H bonds of the ethyl group are closer to the heme iron than those of the Cα (3.5 vs. 4.8 A?). This observation, when coupled to the relative energies of the reaction intermediates, indicates that the positioning of the alkyl group relative to the heme iron may be critical in determining the amount of desaturation that is observed. By mutating a single residue in the active site of CYP199A4 (Phe185) we were able to convert the enzyme into a 4-ethylbenzoic acid desaturase. Engineering a P450 desaturase: The substrate range of CYP199A4 from Rhodopseudomonas palustris was investigated. The partition between the hydroxylation and desaturation activities of 4-ethylbenzoic acid was studied by changing the substrate and by mutation. The activity of CYP199A4 with 4-ethylbenzoic acid was changed to a desaturase by a single mutation at F185. Copyright