13333-86-3

Usage

Uses

Used in Pharmaceutical and Agrochemical Industries:
(BIPHENYL-4-YLOXY)-ACETIC ACID is used as a building block in organic synthesis for the development of various pharmaceuticals and agrochemicals. Its structural attributes make it a valuable starting material for creating new compounds with therapeutic or pesticidal properties.
Used in Organic Synthesis:
(BIPHENYL-4-YLOXY)-ACETIC ACID is utilized as a reagent in the synthesis of other organic compounds, contributing to the creation of a wide range of chemical entities for research and commercial purposes.
Used in Analytical Chemistry:
(BIPHENYL-4-YLOXY)-ACETIC ACID is employed as a reference standard, ensuring the accuracy and reliability of analytical methods in various chemical and biological assays.
Used in Drug Discovery:
Due to its potential pharmacological activities, (BIPHENYL-4-YLOXY)-ACETIC ACID is used in drug discovery processes to identify and develop new therapeutic agents, particularly for conditions such as inflammation and cancer.
Used in Research:
(BIPHENYL-4-YLOXY)-ACETIC ACID is applied in research settings to explore its properties and potential applications, furthering the understanding of its role in chemical and biological systems.

InChI:InChI=1/C14H12O3/c15-14(16)10-17-13-8-6-12(7-9-13)11-4-2-1-3-5-11/h1-9H,10H2,(H,15,16)/p-1

Upstream product

• 3645-61-2 sodium 4-phenylphenoxide 
• 105-36-2 ethyl bromoacetate 
• 92-69-3 4-Phenylphenol 
• 79-08-3 bromoacetic acid 
• 79-14-1 glycolic Acid 
• 1591-31-7 4-iodo-biphenyl 
• 305-53-3 monosodium iodoacetate 
• 79-11-8 chloroacetic acid 
• 54334-74-6 ethyl 2-(biphenyl-4-yloxy)acetate 
• 63472-21-9 3-([1,1'-biphenyl]-4-yloxy)propanoic acid 
• 54334-73-5 methyl 4-biphenyloxyacetate 
• 54334-79-1 (Biphenyl-4-yloxy)-acetic acid tert-butyl ester 
• 107-59-5 tert-Butyl chloroacetate 

Downstream Products

• 1220715-99-0 C₂₆H₂₈BNO₅ 
• 1401223-10-6 2-(biphenyl-4-yloxy)-N-isopropyl-N-((3-phenyl-1,2,4-oxadiazol-5-yl)methyl)acetamide 
• 1415560-92-7 C₂₆H₂₁N₃O₃ 
• 1415560-95-0 2-((biphenyl-4-yloxy)methyl)-1H-benzo[d]imidazole-5-carboxylic acid 
• 1415560-94-9 methyl 2-((biphenyl-4-yloxy)methyl)-1H-benzo[d]imidazole-5-carboxylate 
• 905286-36-4 methyl 2-{[(4-biphenylyloxy)acetyl]amino}-5-methyl-3-thiophenecarboxylate 
• 905286-43-3 methyl 2-{[(4-biphenylyloxy)acetyl]amino}-3-thiophenecarboxylate 
• 905286-34-2 methyl 3-{[(4-biphenylyloxy)acetyl]amino}-4-methyl-2-thiophenecarboxylate 
• 42973-13-7 2-(biphenyl-4-yloxy)acetyl chloride 

Relevant academic research and scientific papers

Discovery of Selective Inhibitors Targeting Acetylcholinesterase 1 from Disease-Transmitting Mosquitoes

Vector control of disease-transmitting mosquitoes is increasingly important due to the re-emergence and spread of infections such as malaria and dengue. We have conducted a high throughput screen (HTS) of 17,500 compounds for inhibition of the essential AChE1 enzymes from the mosquitoes Anopheles gambiae and Aedes aegypti. In a differential HTS analysis including the human AChE, several structurally diverse, potent, and selective noncovalent AChE1 inhibitors were discovered. For example, a phenoxyacetamide-based inhibitor was identified with a 100-fold selectivity for the mosquito over the human enzyme. The compound also inhibited a resistance conferring mutant of AChE1. Structure-selectivity relationships could be proposed based on the enzymes' 3D structures; the hits' selectivity profiles appear to be linked to differences in two loops that affect the structure of the entire active site. Noncovalent inhibitors of AChE1, such as the ones presented here, provide valuable starting points toward insecticides and are complementary to existing and new covalent inhibitors.

(Trifluoromethylselenyl)methylchalcogenyl as Emerging Fluorinated Groups: Synthesis under Photoredox Catalysis and Determination of the Lipophilicity

The synthesis of molecules bearing (trifluoromethylselenyl)methylchalcogenyl groups is described via an efficient two-step strategy based on a metal-free photoredox catalyzed decarboxylative trifluoromethylselenolation with good yields up to 88 %, which raised to 98 % in flow chemistry conditions. The flow methods allowed also to scale up the reaction. The mechanism of this key reaction was studied. The physicochemical characterization of these emerging groups was performed by determining their Hansch–Leo lipophilicity parameters with high values up to 2.24. This reaction was also extended to perfluoroalkylselenolation with yields up to 95 %. Finally, this method was successfully applied to the functionalization of relevant bioactive molecules such as tocopherol or estrone derivatives.

Design and synthesis of α-phenoxy-N-sulfonylphenyl acetamides as Trypanosoma brucei Leucyl-tRNA synthetase inhibitors

Human African trypanosomiasis (HAT), caused by the parasitic protozoa Trypanosoma brucei, is one of the fatal diseases in tropical areas and current medicines are insufficient. Thus, development of new drugs for HAT is urgently needed. Leucyl-tRNA synthetase (LeuRS), a recently clinically validated antimicrobial target, is an attractive target for development of antitrypanosomal drugs. In this work, we report a series of α-phenoxy-N-sulfonylphenyl acetamides as T. brucei LeuRS inhibitors. The most potent compound 28g showed an IC50 of 0.70 μM which was 250-fold more potent than the starting hit compound 1. The structure-activity relationship was also discussed. These acetamides provided a new scaffold and lead compounds for the further development of clinically useful antitrypanosomal agents.

N-aryl 2-aryloxyacetamides as a new class of fatty acid amide hydrolase (FAAH) inhibitors

Fatty acid amide hydrolase (FAAH) is a promising target for the development of drugs to treat neurological diseases. In search of new FAAH inhibitors, we identified 2-(4-cyclohexylphenoxy)-N-(3-(oxazolo[4,5-b]pyridin-2-yl)phenyl)acetamide, 4g, with an IC50 of 2.6 μM as a chemical starting point for the development of potent FAAH inhibitors. Preliminary hit-to-lead optimisation resulted in 2-(4-phenylphenoxy)-N-(3-(oxazolo[4,5-b]pyridin-2-yl)phenyl)acetamide, 4i, with an IC50 of 0.35 μM.

Radical decarboxylative fluorination of aryloxyacetic acids using N-fluorobenzenesulfonimide and a photosensitizer

Fluorinated methoxy arenes are emerging as important motifs in both agrochemicals and pharmaceuticals. A novel technique for the synthesis of monofluoromethoxy arenes through the direct fluorodecarboxylation of carboxylic acids was developed that uses photosensitizers and N-fluorobenzenesulfonimide (NFSI). Utilization of the oxidatively mild fluorine transfer agent NFSI enabled the synthesis of fluoromethyl ethers that were previously inaccessible with decarboxylative fluorinations performed with Selectfluor. Mechanistic studies are consistent with the photosensitizer effecting oxidation of the aryloxyacetic acid.

Direct C-F bond formation using photoredox catalysis

We have developed the first example of a photoredox catalytic method for the formation of carbon-fluorine (C-F) bonds. The mechanism has been studied using transient absorption spectroscopy and involves a key single-electron transfer from the 3MLCT (triplet metal-to-ligand charge transfer) state of Ru(bpy)32+ to Selectfluor. Not only does this represent a new reaction for photoredox catalysis, but the mild reaction conditions and use of visible light also make it a practical improvement over previously developed UV-mediated decarboxylative fluorinations.

Copper(II)-catalyzed hydroxylation of aryl halides using glycolic acid as a ligand

Copper(II)-catalyzed hydroxylation of aryl halides has been developed to afford functionalized phenols. The protocol utilizes the reagent combination of Cu(OH)2, glycolic acid, and NaOH in aqueous DMSO, all of which are cheap, readily available, and easily removable after the reaction. A broad range of aryl iodides and activated aryl bromides were transformed into the corresponding phenols in excellent yields. Moreover, it has been shown that C-O(alkyl)-coupled product, instead of phenol, can be predominantly formed under similar reaction conditions.

Oxadiazole-isopropylamides as potent and noncovalent proteasome inhibitors

Screening of the 50 000 ChemBridge compound library led to the identification of the oxadiazole-isopropylamide 1 (PI-1833) which inhibited chymotrypsin-like (CT-L) activity (IC50 = 0.60 μM) with little effects on the other two major proteasome proteolytic activities, trypsin-like (T-L) and postglutamyl-peptide-hydrolysis-like (PGPH-L). LC-MS/MS and dialysis show that 1 is a noncovalent and rapidly reversible CT-L inhibitor. Focused library synthesis provided 11ad (PI-1840) with CT-L activity (IC50 = 27 nM). Detailed SAR studies indicate that the amide moiety and the two phenyl rings are sensitive toward modifications. Hydrophobic residues, such as propyl or butyl in the para position (not ortho or meta) of the A-ring and a m-pyridyl group as B-ring, significantly improve activity. Compound 11ad (IC50 = 0.37 μM) is more potent than 1 (IC50 = 3.5 μM) at inhibiting CT-L activity in intact MDA-MB-468 human breast cancer cells and inhibiting their survival. The activity of 11ad warrants further preclinical investigation of this class as noncovalent proteasome inhibitors.

Discovery of a novel series of benzimidazole derivatives as diacylglycerol acyltransferase inhibitors

A novel series of benzimidazole derivatives was prepared and evaluated for their diacylglycerol acyltransferase (DGAT) inhibitory activity using microsome from rat liver. Among the newly synthesized compounds, furfurylamine containing benzimidazole carboxamide 10j showed the most potent DGAT inhibitory effect (IC50= 4.4 μM) and inhibited triglyceride formation in HepG2 cells. Furthermore, compound 10j reduced body weight gain of Institute of Cancer Research mice on a high-fat diet and decreased levels of total triglyceride, total cholesterol, and LDL-cholesterol in the blood accompanied with a significant increase in HDL-cholesterol level.

PROTEASOME CHYMOTRYPSIN-LIKE INHIBITION USING PI-1833 ANALOGS

Focused library synthesis and medicinal chemistry on an oxadiazole- isopropylamide core proteasome inhibitor provided the lead compound that strongly inhibits CT-L activity. Structure activity relationship studies indicate the amide moiety and two phenyl rings are sensitive toward synthetic modifications. Only para-substitution in the A-ring was important to maintain potent CT-L inhibitory activity. Hydrophobic residues in the A-ring?s para-position and meta-pyridyl group at the B- ring significantly improved inhibition. The meta-pyridyl moiety improved cell permeability. The length of the aliphatic chain at the para position of the A-ring is critical with propyl yielding the most potent inhibitor, whereas shorter (i.e. ethyl, methyl or hydrogen) or longer (i.e. butyl, propyl and hexyl) chains demonstrating progressively less potency. Introduction of a stereogenic center next to the ether moiety (i.e. substitution of one of the hydrogens by methyl) demonstrated chiral discrimination in proteasome CT-L activity inhibition (the S-enantiomer was 35-40 fold more potent than the R-enantiomer)