57676-50-3

Usage

Appearance

White to off-white solid

Molecular weight

226.08 g/mol

Common uses

Reagent in organic synthesis, particularly in the preparation of pharmaceuticals and other biologically active molecules

Functional groups

Hydrazide (N-NH-CO-R) and bromine-substituted phenyl ring

Reactivity

Versatile nucleophile, useful for halogenation or substitution at specific positions in organic molecules

Upstream product

• 14062-25-0 Ethyl 4-bromophenylacetate 
• 41841-16-1 (4-bromo-phenyl)-acetic acid methyl ester 
• 1878-68-8 2-(4-bromophenyl)-acetic acid 

Downstream Products

• 57676-23-0 2,2'-bis-(4-bromo-benzyl)-4,5,4',5'-tetrahydro-4,4'-(2-oxa-propane-1,3-diyl)-bis-[1,3,4]oxadiazole 
• 78131-94-9 5-(4-bromophenoxy)methyl-1,3,4-oxadiazole-2-thione 
• 893325-57-0 C₁₆H₁₆BrN₃O₂S 
• 891958-94-4 C₁₆H₁₆BrN₃OS 
• 893325-73-0 C₁₆H₁₆BrN₃O₂S 

Relevant academic research and scientific papers

IL4I1 INHIBITORS AND METHODS OF USE

Described herein are compounds of Formula I or a pharmaceutically acceptable salt thereof. The compounds of Formula I act as IL4I1 inhibitors and can be useful in preventing, treating or acting as a remedial agent for IL4I1-related diseases.

Acetylcholinesterase inhibition activity of some quinolinyl substituted triazolothiadiazole derivatives

A series of aralkanoic acids was converted into aralkanoic acid hydrazides through their esters formation. The aralkanoic acid hydrazides upon treatment with carbon disulfide and methanolic potassium hydroxide yielded potassium dithiocarbazinate salts, which on refluxing with aqueous hydrazine hydrate yielded 5-aralkyl-4-amino-3-mercapto-1,2,4-triazoles. The target compounds, 3-aralkyl-6-(substitutedquinolinyl) [1,2,4]triazolo[3,4-b][1,3,4]thiadiazoles, were synthesized by condensing various quinolinyl substituted carboxylic acids with 5-aralkyl-4-amino-3-mercapto-1,2,4-triazoles in phosphorus oxychloride. The structures of the newly synthesized triazolothiadiazoles were characterized by IR, 1H NMR, 13C NMR, and elemental analysis studies. The structure of one of the 5-aralkyl-4-amino-3-mercapto-1,2,4-triazoles was unambiguously deduced by single crystal X-ray diffraction analysis. All the synthesized compounds were screened for their acetylcholinesterase inhibition activities. Four of the triazolothiadiazoles exhibited excellent acetylcholinesterase inhibition activities as compared to the reference inhibitor.

Influence of the diversified structural variations at the imine functionality of 4-bromophenylacetic acid derived hydrazones on alkaline phosphatase inhibition: Synthesis and molecular modelling studies

Alkaline phosphatase (AP) isozymes are present in a wide range of species from bacteria to humans with an ability to dephosphorylate and transphosphorylate a wide range of substrates. In humans, four AP isozymes have been identified such as tissue-nonspecific (TNAP), intestinal (IAP), placental (PLAP) and germ cell (GCAP) APs. Modulation of the activity of the different AP isozymes may have therapeutic implications in distinct diseases and cellular processes. To identify potent inhibitors of APs, a diverse range of 4-bromophenylacetic acid derived hydrazone derivatives has been synthesized and characterized by spectro-analytical methods and, in the case of 4i and 4q, by single crystal X-ray diffraction analysis. Among the tested series, several compounds were identified as lead candidates showing IC50 values from micro to nanomolar ranges. Compound 4k displayed exceptional activity with an IC50 value of 10 nM against h-IAP. This inhibitory effect is ～10000-fold more potent than the standard drug l-phenylalanine. Compounds 4p, 4g and 4e were potent inhibitors of TNAP, PLAP and GCAP, respectively. Molecular docking studies of the respective potent inhibitors have been carried out to rationalize the important binding modes of the most active inhibitors.

Identification of novel urease inhibitors by high-throughput virtual and in vitro screening

Ureases are important in both agriculture and human health. Bacterial ureases are directly involved in many farm-field problems and pathological conditions. Here, we report a structure-based virtual screening of an in-house compound bank of about 6000 molecular entities by computational docking and binding free energy calculations followed by in vitro screening. Applied protocol leads to the identification of novel urease inhibitors, which can serve as starting points for structural optimization.