69770-20-3

Usage

Uses

Used in Pharmaceutical Industry:
3-(4-Chlorophenoxy)benzaldehyde is used as a key intermediate in the synthesis of various pharmaceutical compounds, specifically for the creation of fatty acid amide hydrolase inhibitors bearing spirocyclic diamine cores. These inhibitors have potential applications in treating a range of conditions, including neurological disorders and cancer.
Additionally, 3-(4-Chlorophenoxy)benzaldehyde is used as a research compound for investigating its anti-tumor properties. Its potential to contribute to the development of novel anti-cancer drugs makes it a valuable asset in the ongoing fight against cancer.

InChI:InChI=1/C13H9ClO2/c14-11-4-6-12(7-5-11)16-13-3-1-2-10(8-13)9-15/h1-9H

Upstream product

• 3132-99-8 m-bromobenzoic aldehyde 
• 106-48-9 4-chloro-phenol 
• 146800-14-8 tris(3-formylphenyl)bismuthine 
• 67437-93-8 2-(3-bromophenyl)-[1,3]dioxane 
• 87199-16-4 3-Formylphenylboronic acid 

Downstream Products

• 135473-72-2 {Amino-[3-(4-chloro-phenoxy)-phenyl]-methyl}-phosphonic acid 
• 129764-91-6 3-(4-chlorophenoxy)benzoate 
• 213192-54-2 3-amino-3-[3-(4-chlorophenoxy)phenyl]propionic acid 
• 328543-17-5 1-[3-(4-Chlorophenoxy)-phenyl]-8,9-dihydro-7H-2,7,9a-triaza-benzo[cd]azulen-6-one 
• 149609-93-8 Ethyl 3-(3-(4-chlorphenoxy)phenyl)propynoate 
• 108384-90-3 ethyl 5-[3-(4-chlorophenoxy)phenyl]-3-oxo-4-pentenoate 
• 56911-60-5 1-[3-(4-chlorophenoxy)phenyl] ethanol 
• 188953-47-1 C₁₇H₁₅ClO₃ 
• 1230021-77-8 tert-butyl 4-(3-(4-chlorophenoxy)benzyl)piperazine-1-carboxylate 
• 1289080-00-7 5-bromo-3-{3-[3-(4-chlorophenoxy)-phenyl]acryloyl}-2-hydroxybenzoic acid 
• 1394894-48-4 C₂₂H₂₂ClN₅O₂*C₂HF₃O₂ 
• 1230019-64-3 4-[3-(4-chloro-phenoxy)-benzyl]-piperazine-1-carboxylic acid (1H-indazol-7-yl)-amide 
• 1415729-12-2 C₂₅H₂₄ClN₅O₂ 
• 1093209-18-7 C₂₅H₂₃ClN₄O₃ 

Relevant academic research and scientific papers

Structure-aided optimization of non-nucleoside M. tuberculosis thymidylate kinase inhibitors

Mycobacterium tuberculosis thymidylate kinase (MtTMPK) has emerged as an attractive target for rational drug design. We recently investigated new families of non-nucleoside MtTMPK inhibitors in an effort to diversify MtTMPK inhibitor chemical space. We here report a new series of MtTMPK inhibitors by combining the Topliss scheme with rational drug design approaches, fueled by two co-crystal structures of MtTMPK in complex with developed inhibitors. These efforts furnished the most potent MtTMPK inhibitors in our assay, with two analogues displaying low micromolar MIC values against H37Rv Mtb. Prepared inhibitors address new sub-sites in the MtTMPK nucleotide binding pocket, thereby offering new insights into its druggability. We studied the role of efflux pumps as well as the impact of cell wall permeabilizers for selected compounds to potentially provide an explanation for the lack of correlation between potent enzyme inhibition and whole-cell activity.

Cinnamonitrile adjuvants restore susceptibility to β-lactams against methicillin-resistant staphylococcus aureus

β-Lactams are used routinely to treat Staphylococcus aureus infections. However, the emergence of methicillin-resistant S. aureus (MRSA) renders them clinically precarious. We describe a class of cinnamonitrile adjuvants that restore the activity of oxacillin (a penicillin member of the β-lactams) against MRSA. The lead adjuvants were tested against six important strains of MRSA, one vancomycin-intermediate S. aureus (VISA) strain, and one linezolid-resistant S. aureus strain. Five compounds out of 84 total compounds showed broad potentiation. At 8 μM (E)-3-(5-(3,4-dichlorobenzyl)-2-(trifluoromethoxy)phenyl)-2-(methylsulfonyl)acrylonitrile (26) potentiated oxacillin with a >4000-fold reduction of its MIC (from 256 to 0.06 mg·L-1). This class of adjuvants holds promise for reversal of the resistance phenotype of MRSA.

Probing the Hydrophobic Binding Pocket of G-Protein-Coupled Lysophosphatidylserine Receptor GPR34/LPS1 by Docking-Aided Structure-Activity Analysis

The ligands of certain G-protein-coupled receptors (GPCRs) have been identified as endogenous lipids, such as lysophosphatidylserine (LysoPS). Here, we analyzed the molecular basis of the structure-activity relationship of ligands of GPR34, one of the LysoPS receptor subtypes, focusing on recognition of the long-chain fatty acid moiety by the hydrophobic pocket. By introducing benzene ring(s) into the fatty acid moiety of 2-deoxy-LysoPS, we explored the binding site's preference for the hydrophobic shape. A tribenzene-containing fatty acid surrogate with modifications of the terminal aromatic moiety showed potent agonistic activity toward GPR34. Computational docking of these derivatives with a homology modeling/molecular dynamics-based virtual binding site of GPR34 indicated that a kink in the benzene-based lipid surrogates matches the L-shaped hydrophobic pocket of GPR34. A tetrabenzene-based lipid analogue bearing a bulky tert-butyl group at the 4-position of the terminal benzene ring exhibited potent GPR34 agonistic activity, validating the present hydrophobic binding pocket model.

Conformational Constraint of the Glycerol Moiety of Lysophosphatidylserine Affords Compounds with Receptor Subtype Selectivity

Lysophosphatidylserine (LysoPS) is an endogenous lipid mediator that specifically activates membrane proteins of the P2Y and its related families of G protein-coupled receptors (GPCR), GPR34 (LPS1), P2Y10 (LPS2), and GPR174 (LPS3). Here, in order to increase potency and receptor selectivity, we designed and synthesized LysoPS analogues containing the conformational constraints of the glycerol moiety. These reduced structural flexibility by fixation of the glycerol framework of LysoPS using a 2-hydroxymethyl-3-hydroxytetrahydropyran skeleton, and related structures identified compounds which exhibited high potency and selectivity for activation of GPR34 or P2Y10. Morphing of the structural shape of the 2-hydroxymethyl-3-hydroxytetrahydropyran skeleton into a planar benzene ring enhanced the P2Y10 activation potentcy rather than the GPR34 activation.

Synthesis of highly functionalized diaryl ethers by copper-mediated O-arylation of phenols using trivalent arylbismuth reagents

Highly functionalized diaryl ethers were prepared by copper(II) acetate mediated O-arylation reaction of phenols using trivalent organobismuthanes. The reaction is performed under simple conditions and tolerates a wide diversity of functional groups on the phenol and on the organobismuth reagent. Substoichiometric amounts of catalyst can be used by performing the reaction under an oxygen atmosphere. The N-arylation of pyridones is also reported. Highly functionalized diaryl ethers were prepared by a copper(II) acetate mediated O-arylation reaction of phenols using trivalent organobismuthanes (see scheme). The reaction is performed under simple conditions and tolerates a wide diversity of functional groups on the phenol and on the organobismuth reagent. Substoichiometric amounts of catalyst can be used by performing the reaction under an oxygen atmosphere. The N-arylation of pyridones is also reported. FG=functional group.

Design and synthesis of l- and d-phenylalanine derived rhodanines with novel C5-arylidenes as inhibitors of HCV NS5B polymerase

Hepatitis C virus (HCV) NS5B polymerase is a key target for anti-HCV therapeutics development. Herein, we report the synthesis and in vitro evaluation of anti-NS5B polymerase activity of a molecular hybrid of our previously reported lead compounds 1 (IC50 = 7.7 μM) and 2 (IC50 = 10.6 μM) as represented by hybrid compound 27 (IC 50 = 6.7 μM). We have explored the optimal substituents on the terminal phenyl ring of the 3-phenoxybenzylidene moiety in 27, by generating a set of six analogs. This resulted in the identification of compound 34 with an IC50 of 2.6 μM. To probe the role of stereochemistry towards the observed biological activity, we synthesized and evaluated the d-isomers 41 (IC50 = 19.3 μM) and 45 (IC50 = 5.4 μM) as enantiomers of the l-isomers 27 and 34, respectively. The binding site of compounds 32 and 34 was mapped to palm pocket-I (PP-I) of NS5B. The docking models of 34 and 45 within the PP-I of NS5B were investigated to envisage the molecular mechanism of inhibition.

Arylamidoalkyl-N-hydroxyurea compounds having lipoxygenase inhibitory activity

The present invention provides certain (substituted carbocyclic aryl)amidoalkyl- and (substituted heterocyclic aryl)amidoalkyl-N-Hydroxy urea compounds which inhibit lipoxygenase enzyme activity and are thus useful in the treatment of allergic and inflammatory disease states.

ARYLAMIDOALKYL-N-HYDROXYUREA COMPOUNDS HAVING LIPOXYGENASE INHIBITORY ACTIVITY

The present invention provides certain (substituted carbocyclic aryl)amidoalkyl and (substituted hetero cyclic aryl) amido alkyl-N-Hydroxy urea compounds which inhibit lipoxygenase enzyme activity and are thus useful in the treatment of allergic and inflammatory disease states

PHARMACOLOGICALLY ACTIVE TRIAZINONES

The compounds are substituted 1,2,4-triazin-5-ones which are histamine H 2-antagonists. Two specific compounds of the present invention are 3-2-(5-methyl-4-imidazolylmethylthio)ethylamino!-6-(3-methoxybenzyl)-1,2, 4-tr iazin-5-one and 3-2-(5-methyl-4-imidazolylmethylthio)ethylamino!-6-(3-pyridylmethyl)-1,2,4-tr iazin-5-one.