100960-18-7

Upstream product

• 99-60-5 2-chloro-4-nitrobenzoic acid 
• 16017-69-9 ethyl-2-chloro-4-amino-benzoate 
• 46004-37-9 methyl 4-amino-2-chlorobenzoate 
• 2457-76-3 4-amino-2-chlorobenzoic acid 
• 85953-29-3 methyl 2-chloro-4-fluorobenzoate 

Relevant academic research and scientific papers

Design and optimization of N-acylhydrazone pyrimidine derivatives as E. coli PDHc E1 inhibitors: Structure-activity relationship analysis, biological evaluation and molecular docking study

By targeting the thiamin diphosphate (ThDP) binding site of Escherichia coli (E. coli) pyruvate dehydrogenase multienzyme complex E1 (PDHc E1), a series of novel ‘open-chain’ classes of ThDP analogs A, B, and C with N-acylhydrazone moieties was designed and synthesized to explore their activities against E. coli PHDc E1 in vitro and their inhibitory activity against microbial diseases were further evaluated in vivo. As a result, A1–23 exhibited moderate to potent inhibitory activities against E. coli PDHc E1 (IC50 = 0.15–23.55 μM). The potent inhibitors A13, A14, A15, C2, had strong inhibitory activities with IC50 values of 0.60, 0.15, 0.39 and 0.34 μM against E. coli PDHc E1 and with good enzyme-selective inhibition between microorganisms and mammals. Especially, the most powerful inhibitor A14 could 99.37% control Xanthimonas oryzae pv. Oryzae. Furthermore, the binding features of compound A14 within E. coli PDHc E1 were investigated to provide useful insights for the further construction of new inhibitor by molecular docking, site-directed mutagenesis, and enzymatic assays. The results indicated that A14 had most powerful inhibition against E. coli PDHc E1 due to the establishment of stronger interaction with Glu571, Met194, Glu522, Leu264 and Phe602 at active site of E.coli PDHc E1. It could be used as a lead compound for further optimization, and may have potential as a new microbicide.

Four substituted benzohydrazides: Hydrogen-bonded structures in one, two and three dimensions

The molecules of 2,6-dichlorobenzohydrazide, C7H 6Cl2N2O, are linked into simple chains by a single N-H...O hydrogen bond, while in the isomeric compound 2,4-dichlorobenzo-hydrazide, the molecules are linked by

Biological evaluation and molecular docking studies of 4-aminobenzohydrazide derivatives as cholinesterase inhibitors

Nowadays, inhibition of the acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) enzymes have emerged as an encouraging approach in the treatment of dementia and remission of symptoms of Alzheimer's disease. Therefore, inhibition of cholinesterase

Purification of peroxidase enzyme from radish species in fast and high yield with affinity chromatography technique

In this study, an effective single step affinity method is presented for purifying plant peroxidase (POD) enzymes from radish species. This method make possible to purify the enzymes in high yield and purity. Briefly, 10 different 4-amino benzohydrazide d