36372-16-4

Usage

InChI:InChI=1/C14H11BrO2/c15-12-8-6-11(7-9-12)14(16)10-17-13-4-2-1-3-5-13/h1-9H,10H2

Upstream product

• 99-73-0 para-bromophenacyl bromide 
• 108-95-2 phenol 
• 721-04-0 2-phenoxy-1-phenylethanone 
• 19513-79-2 2-phenoxy-1-p-tolylethanone 
• 73014-18-3 2-<2-Hydroxy-phenyl>-1-phenoxy-aethanon-(2) 
• 99-90-1 para-bromoacetophenone 

Downstream Products

• 117886-83-6 (4-bromo-phenyl)-(1H-tetrazol-5-yl)-ketone 
• 721-04-0 2-phenoxy-1-phenylethanone 
• 99-90-1 para-bromoacetophenone 
• 125734-57-8 1-(4-bromophenyl)-2-phenoxyethan-1-ol 
• 250279-07-3 3-(4-bromophenyl)-1-benzofuran 
• 29263-70-5 1-([1,1'-biphenyl]-4-yl)-2-phenoxyethan-1-one 
• 19513-79-2 2-phenoxy-1-p-tolylethanone 
• 73014-18-3 2-<2-Hydroxy-phenyl>-1-phenoxy-aethanon-(2) 
• 6846-12-4 4-bromo-N-phenyl-benzamide 
• 108-95-2 phenol 
• 14966-77-9 6-(4-bromo-phenyl)-3,4-diphenyl-2H-pyran-2-one 
• 32175-23-8 (E)-phenyl 2,3-diphenyl acrylate 
• 125758-77-2 5-<4-<1-<(tert-butyldimethylsilyl)oxy>-2-phenoxyethyl>benzyl>thiazolidine-2,4-dione 
• 141221-12-7 5-<4-<1-<(tert-butyldimethylsilyl)oxy>-2-phenoxyethyl>phenylmethylene>thiazolidine-2,4-dione 

Relevant academic research and scientific papers

Cobalt-Catalyzed Reductive C-O Bond Cleavage of Lignin β-O-4 Ketone Models via in Situ Generation of the Cobalt-Boryl Species

An efficient and mild method for reductive C-O bond cleavage of lignin β-O-4 ketone models was developed to afford the corresponding ketones and phenols with PDI-CoCl2 as the precatalyst and diboron reagent as the reductant. The synthetic utility of the methodology was demonstrated by depolymerization of a polymeric model and gram-scale transformation. Mechanistic studies suggested that this transformation involves steps of carbonyl insertion, 1,2-Brook type rearrangement, β-oxygen elimination, and rate-limiting regeneration of the catalytic active Co-B species.

Copper-catalyzed synthesis of benzanilides from lignin model substrates 2-phenoxyacetophenones under an air atmosphere

The synthesis of chemicals from biomass-derived compounds is an interesting and challenging topic. In this work, using the lignin-derived 2-phenoxyacetophenones as the feedstock we present a novel approach for the synthesis of benzanilides via the reaction of 2-phenoxyacetophenones with anilines catalyzed by CuCl2 in DMSO at 120 °C under an air atmosphere. This approach has wide scope for 2-phenoxyacetophenones and anilines, and various benzanilides accompanied by the corresponding phenols could be obtained in high yields via changing the 2-phenoxyacetophenones and anilines. The reaction mechanism study indicated that the oxidative cleavage of the C-C bond in 2-phenoxyacetophenones and the formation of a C-N bond occurred simultaneously in the reaction process, resulting in the formation of benzanilides together with phenols.

Synthesis and structure-activity relationship study of a new series of antiparasitic aryloxyl thiosemicarbazones inhibiting Trypanosoma cruzi cruzain

The discovery of new antiparasitic compounds against Trypanosoma cruzi, the etiological agent of Chagas disease, is necessary. Novel aryloxy/aryl thiosemicarbazone-based conformationally constrained analogs of thiosemicarbazones (1) and (2) were developed

Structural design, synthesis and structure-activity relationships of thiazolidinones with enhanced anti-Trypanosoma cruzi activity

Pharmacological treatment of Chagas disease is based on benznidazole, which displays poor efficacy when administered during the chronic phase of infection. Therefore, the development of new therapeutic options is needed. This study reports on the structural design and synthesis of a new class of anti-Trypanosoma cruzi thiazolidinones (4 a-p). (2-[2-Phenoxy-1-(4-bromophenyl) ethylidene)hydrazono]-5-ethylthiazolidin-4-one (4 h) and (2-[2-phenoxy-1-(4- phenylphenyl)ethylidene)hydrazono]-5-ethylthiazolidin-4-one (4 l) were the most potent compounds, resulting in reduced epimastigote proliferation and were toxic for trypomastigotes at concentrations below 10 μM, while they did not display host cell toxicity up to 200 μM. Thiazolidinone 4 h was able to reduce the in vitro parasite burden and the blood parasitemia in mice with similar potency to benznidazole. More importantly, T. cruzi infection reduction was achieved without exhibiting mouse toxicity. Regarding the molecular mechanism of action, these thiazolidinones did not inhibit cruzain activity, which is the major trypanosomal protease. However, investigating the cellular mechanism of action, thiazolidinones altered Golgi complex and endoplasmic reticulum (ER) morphology, produced atypical cytosolic vacuoles, as well as induced necrotic parasite death. This structural design employed for the new anti-T. cruzi thiazolidinones (4 a-p) led to the identification of compounds with enhanced potency and selectivity compared to first-generation thiazolidinones. These compounds did not inhibit cruzain activity, but exhibited strong antiparasitic activity by acting as parasiticidal agents and inducing a necrotic parasite cell death. Stop the cycle! The attachment of an aryl ring to the iminic carbon produced thiazolidinones that are conformationally more restricted than first-generation thiazolidinones. This enhanced the potency of antiparasitic thiazolidinones, as observed under treatment with compound 4 h where parasite development and invasion in host cells were substantially reduced. Copyright

Chiral epoxides via borane reduction of 2-haloketones catalyzed by spiroborate ester: Application to the synthesis of optically pure 1,2-hydroxy ethers and 1,2-azido alcohols

An enantioselective borane-mediated reduction of a variety of 2-haloketones with 10% spiroaminoborate ester 1 as catalyst is described. By a simple basic workup of 2-halohydrins, optically active epoxides are obtained in high yield and with excellent enantiopurity (up to 99% ee). Ring-opening of oxiranes with phenoxides or sodium azide is investigated under different reaction conditions affording nonracemic 1,2-hydroxy ethers and 1,2-azido alcohols with excellent enantioselectivity (99% ee) and in good to high chemical yield. 2011 American Chemical Society.

DERIVATIVES OF 4-(2-AMINO-1-HYDROXYETHYL)PHENOL AS AGONISTS OF THE β2 ADRENERGIC RECEPTOR

The present invention provides a Compound of formula (I), wherein: R1 is a group selected from -CH2OH,-NH(CO)H; and R2 is a hydrogen atom; or R1 together with R2 form the group -NH-C(O)-CH=CH-, wherei

Biphenyl sulfonyl aryl carboxylic acids useful in the treatment of insulin resistance and hyperglycemia

This invention provides compounds of Formula I having the structure wherein A, Q, R3, and R4 are as defined hereinbefore in the specification, or a pharmaceutically acceptable salt thereof, which are useful in treating metabolic disorders related to insulin resistance or hyperglycemia.

Biphenyl oxo-acetic acids useful in the treatment of insulin resistance and hyperglycemia

This invention provides compounds of Formula I having the structure wherein A, R3, R4, and R5are as defined hereinbefore in the specification, or a pharmaceutically acceptable salt thereof, which are useful in treating metabolic disorders related to insulin resistance or hyperglycemia.

Novel benzofuran and benzothiophene biphenyls as inhibitors of protein tyrosine phosphatase 1B with antihyperglycemic properties

Insulin resistance in the liver and peripheral tissues, together with a pancreatic cell defect, are the common causes of Type 2 diabetes. It is now appreciated that insulin resistance can result from a defect in the insulin receptor signaling system, at a site post binding of insulin to its receptor. Protein tyrosine phosphatases (PTPases) have been shown to be negative regulators of the insulin receptor. Inhibition of PTPases may be an effective method in the treatment of Type 2 diabetes. We have identified two novel series of benzofuran/benzothiophene biphenyl oxo-acetic acids and sulfonyl- salicylic acids as potent inhibitors of PTP1B with good oral antihyperglycemic activity. To assist in the design of these inhibitors, crystallographic studies have attempted to identify enzyme inhibitor interactions. Resolution of crystal complexes has suggested that the inhibitors bind to the enzyme active site and are held in place through hydrogen bonding and van der Waals interactions formed within two hydrophobic pockets. In the oxo-acetic acid series, hydrophobic substitutents at position-2 of the benzofuran/benzothiophene biphenyl framework interacted with Phe182 of the catalytic site and were very critical to the intrinsic activity of the molecule. The hydrophobic region of the catalytic-site pocket was exploited and taken advantage by hydrophobic substituents at either the α-carbon or the ortho aromatic positions of the oxo-acetic acid moiety. Similar ortho aromatic substitutions on the salicylic acid-type inhibitors had no effect, primarily due to the different orientation of these inhibitors in the catalytic site. The most active inhibitors of both series inhibited recombinant human PTP1B with phosphotyrosyl dodecapeptide TRDI(P)YETD(P)Y(P)YRK as the source of the substrate with IC50 values in the range of 20-50 nM. Compound 68 was one of the most active compounds in vivo, normalizing plasma glucose levels at the 25 mg/kg dose (po) and the 1 mg/kg dose (ip). Compound 68 was also selective against several other PTPases.

Novel Thiazolidine-2,4-diones as Potent Euglycemic Agents

A new series of thiazolidine-2,4-diones was obtained by replacing the ether function of englitazone with various functional groups, i.e., a ketone, alcohol, or olefin moiety.These compounds lower blood glucose levels in the genetically obese and insulin-r