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2-Hydroxy-4-phenylbenzoic acid, with the CAS number 4482-27-3, is an organic compound belonging to the class of salicylic acids. It features a hydroxyl group at the 2nd position and a phenyl group at the 4th position of the benzene ring. 2-Hydroxy-4-phenylbenzoic acid is known for its potential applications in the pharmaceutical and chemical industries due to its unique structural properties.

4482-27-3

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4482-27-3 Usage

Uses

Used in Pharmaceutical Industry:
2-Hydroxy-4-phenylbenzoic acid is used as a building block for the synthesis of chromones, which are known to act as tyrosine phosphatase inhibitors. These inhibitors play a crucial role in regulating various cellular processes, including signal transduction and gene expression, making them valuable in the development of therapeutic agents for various diseases.
2-Hydroxy-4-phenylbenzoic acid is also used as a potential anti-inflammatory drug due to its salicylic acid nature. It can help in reducing inflammation and pain, making it a promising candidate for the development of new medications to treat conditions like arthritis and other inflammatory disorders.
Used in Chemical Industry:
In the chemical industry, 2-Hydroxy-4-phenylbenzoic acid serves as an important intermediate for the synthesis of various compounds with diverse applications. Its unique structure allows for further functionalization and modification, enabling the creation of new molecules with specific properties and uses in different fields, such as materials science, agrochemicals, and dyes.

Check Digit Verification of cas no

The CAS Registry Mumber 4482-27-3 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 4,4,8 and 2 respectively; the second part has 2 digits, 2 and 7 respectively.
Calculate Digit Verification of CAS Registry Number 4482-27:
(6*4)+(5*4)+(4*8)+(3*2)+(2*2)+(1*7)=93
93 % 10 = 3
So 4482-27-3 is a valid CAS Registry Number.

4482-27-3SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 19, 2017

Revision Date: Aug 19, 2017

1.Identification

1.1 GHS Product identifier

Product name 2-hydroxy-4-phenylbenzoic acid

1.2 Other means of identification

Product number -
Other names 2-Hydroxy-4-phenyl-benzoesaeure

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:4482-27-3 SDS

4482-27-3Relevant academic research and scientific papers

Bi-aryl analogues of salicylic acids: Design, synthesis and sar study to ameliorate endoplasmic reticulum stress

Kim, Ye Eun,Kim, Dong Hwan,Choi, Ami,Jang, Seoul,Jeong, Kwiwan,Kim, Young-Mi,Nam, Tae-Gyu

, p. 3593 - 3604 (2021/08/30)

Introduction: Endoplasmic reticulum (ER) stress condition is characterized as the accu-mulation of misfolded or unfolded proteins in lumen of ER. This condition has been implicated in various diseases and pathologies including β-cell apoptosis, Alzheimer’s disease and atherosclerosis. We have reported that hydroxynaphthoic acids (HNA), naphtha-lene analogues of salicylic acid (SA), reduced ER stress. In this study, we explored structural modification to bi-aryl analogues of SA. Methods: Palladium-catalyzed cross-coupling was applied to synthesize bi-aryl analogues of SA. Anti-ER stress activity was monitored by using our cell-based assay system where ER stress is induced by tunicamycin. To monitor ER stress markers, ER stress was induced physiologically relevant palmitate system. Results: Many analogues decreased ER stress signal induced by tunicamycin. Compounds creating dihedral angle between Ar group and SA moiety generally increased the activity but gave some cytotoxicity to indicate the crucial role of flat conformation of aromatic region. The best compound (16e) showed up to almost 6-fold and 90-fold better activity than 3-HNA and tauro-ursodeoxycholic acid, positive controls, respectively. ER stress markers such as p-PERK and p-JNK were accordingly decreased in Western blotting upon treatment of 16e under palmitate-induced condition. Conclusion: Anti-ER stress activity and toxicity profile of bi-aryl analogues of SA could provide a novel platform for potential therapy for protein misfolding diseases.

Diflunisal Derivatives as Modulators of ACMS Decarboxylase Targeting the Tryptophan-Kynurenine Pathway

Yang, Yu,Borel, Timothy,De Azambuja, Francisco,Johnson, David,Sorrentino, Jacob P.,Udokwu, Chinedum,Davis, Ian,Liu, Aimin,Altman, Ryan A.

, p. 797 - 811 (2021/01/13)

In the kynurenine pathway for tryptophan degradation, an unstable metabolic intermediate, α-amino-β-carboxymuconate-?-semialdehyde (ACMS), can nonenzymatically cyclize to form quinolinic acid, the precursor for de novo biosynthesis of nicotinamide adenine dinucleotide (NAD+). In a competing reaction, ACMS is decarboxylated by ACMS decarboxylase (ACMSD) for further metabolism and energy production. Therefore, the inhibition of ACMSD increases NAD+ levels. In this study, an Food and Drug Administration (FDA)-approved drug, diflunisal, was found to competitively inhibit ACMSD. The complex structure of ACMSD with diflunisal revealed a previously unknown ligand-binding mode and was consistent with the results of inhibition assays, as well as a structure-activity relationship (SAR) study. Moreover, two synthesized diflunisal derivatives showed half-maximal inhibitory concentration (IC50) values 1 order of magnitude better than diflunisal at 1.32 ± 0.07 μM (22) and 3.10 ± 0.11 μM (20), respectively. The results suggest that diflunisal derivatives have the potential to modulate NAD+ levels. The ligand-binding mode revealed here provides a new direction for developing inhibitors of ACMSD.

Fragment-based discovery of potent inhibitors of the anti-apoptotic MCL-1 protein

Petros, Andrew M.,Swann, Steven L.,Song, Danying,Swinger, Kerren,Park, Chang,Zhang, Haichao,Wendt, Michael D.,Kunzer, Aaron R.,Souers, Andrew J.,Sun, Chaohong

, p. 1484 - 1488 (2014/03/21)

Apoptosis is regulated by the BCL-2 family of proteins, which is comprised of both pro-death and pro-survival members. Evasion of apoptosis is a hallmark of malignant cells. One way in which cancer cells achieve this evasion is thru overexpression of the pro-survival members of the BCL-2 family. Overexpression of MCL-1, a pro-survival protein, has been shown to be a resistance factor for Navitoclax, a potent inhibitor of BCL-2 and BCL-XL. Here we describe the use of fragment screening methods and structural biology to drive the discovery of novel MCL-1 inhibitors from two distinct structural classes. Specifically, cores derived from a biphenyl sulfonamide and salicylic acid were uncovered in an NMR-based fragment screen and elaborated using high throughput analog synthesis. This culminated in the discovery of selective and potent inhibitors of MCL-1 that may serve as promising leads for medicinal chemistry optimization efforts.

Tailored design of palladium species grafted on an amino functionalized organozinc coordination polymer as a highly pertinent heterogeneous catalyst

Choudhary,Nishimura,Ebitani

, p. 18687 - 18696 (2014/12/10)

The design of a highly active and stable heterogeneous palladium catalyst is gaining a lot of attention because of its increasing importance in the organic syntheses of commodity chemicals. Herein, we report the tailored synthesis of palladium species grafted on a highly stable amino functionalized organozinc coordination polymer (denoted as Pd/AZC) and its extraordinary catalytic performances in the Suzuki-Miyaura coupling (SMC) reaction. It achieved the highest turnover number of 2106 720 (>99% yield) in air among the most reported palladium catalysts for the SMC reaction of bromobenzene. The as-prepared Pd/AZC composite is also successfully applied for the catalysis of Mizoroki-Heck coupling, hydrogenation of nitro, and -CC- functional groups. Since the developed AZC support has thermal stability at least up to 573 K, it possesses high potential for grafting various metal species as catalytically active centers for a wide range of metal-catalyzed reactions. This journal is

Selectivity in the photo-Fenton and photocatalytic hydroxylation of biphenyl-4-carboxylic acid and derivatives (viz. 4-phenylsalicylic acid and 5-phenylsalicylic acid)

Hathway, Timothy,Chernyshov, Deborah Lipman,Jenks, William S.

supporting information, p. 1151 - 1156 (2013/01/09)

The selectivity of hydroxylation of the distal rings of 4-phenylbenzoic acid, 4-phenylsalicylic acid, and 5-phenylsalicylic acid were determined using partial TiO2-mediated photocatalytic degradation and photo-Fenton conditions. This separation of the binding site from the phenyl group being hydroxylated allows a less-biased evaluation. The hydroxylation regiochemistry behaves as qualitatively expected for an electrophilic reaction, given the assumption that 4-carboxyphenyl is a slightly electron-withdrawing substituent. Selectivity for hydroxylation of the distal phenyl in 4- and 5-phenylsalicylic acid is reversed, due to the reversal of the electronic demand, while adsorption to the TiO2 surface is assumed to be analogous for the two structures. Copyright

Synthesis, activity and molecular modeling of a new series of chromones as low molecular weight protein tyrosine phosphatase inhibitors

Forghieri, Marco,Laggner, Christian,Paoli, Paolo,Langer, Thierry,Manao, Giampaolo,Camici, Guido,Bondioli, Lucia,Prati, Fabio,Costantino, Luca

experimental part, p. 2658 - 2672 (2009/09/08)

Protein tyrosine phosphatases (PTP) are crucial elements in eukaryotic signal transduction. Several reports suggested that the LMW-PTP family has oncogenic relevance. Moreover, LMW-PTP has been recognized as a negative regulator of insulin-mediated mitotic and metabolic signaling. Thus, inhibition of the LMW-PTP can be considered an attractive approach for the design of new therapeutic agents for the treatment of type II diabetes and for new antitumoral drugs. To date very few (and weak) inhibitors of LMW-PTP have been identified. On the basis of the reported weak activity of some flavonoids on phosphatases, we discovered a lead that originated a new class of highly active LMW-PTP inhibitors; these compounds inhibit also PTP-1B and are active in cellular assays. Docking experiments and SAR highlighted the possible binding mode of these compounds to the enzyme, putting the background for the future optimization of their inhibitory activity and selectivity towards the closely related enzyme PTP-1B.

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