82859-76-5

Upstream product

• 99-76-3 methyl 4-hydroxylbenzoate 
• 89-95-2 2-methyl-benzyl alcohol 
• 5351-23-5 4-hydroxybenzoic acid hydrazide 
• 90-02-8 salicylaldehyde 

Downstream Products

• 1261290-21-4 [Cu((E)-N'-(2-hydroxybenzylidene)-4-(hydroxybenzohydrazide(-1H))(NO₃)](H₂O) 
• 1261290-24-7 [(Cu((E)-N'-(2-hydroxybenzylidene)-4-(hydroxybenzohydrazide(-1H))(Me₂NCO))]2 

Relevant academic research and scientific papers

Structure-based design, synthesis, biological evaluation and molecular docking study of 4-hydroxy-n'-methylenebenzohydrazide derivatives acting as tyrosinase inhibitors as potentiate anti-melanogenesis activities

Background: Melanogenesis is a process of melanin synthesis, which is a primary response for the pigmentation of human skin. Tyrosinase is a key enzyme, which catalyzes a rate-limiting step of the melanin formation. Natural products have shown potent inhibitors, but some of these possess toxicity. Numerous synthetic inhibitors have been developed in recent years may lead to the potent anti– tyrosinase agents. Objective: A number of 4-hydroxy-N'-methylenebenzohydrazide analogues with related structure to chalcone and tyrosine were constructed with various substituents at the benzyl ring of the mole-cule and evaluate as a tyrosinase inhibitor. In addition, computational analysis and metal chelating potential have been evaluated. Method: Design and synthesized compounds were evaluated for activity against mushroom ty-rosinase. The metal chelating capacity of the potent compound was examined using the mole ratio method. Molecular docking of the synthesized compounds was carried out into the tyrosine active site. Result: Novel 4-hydroxy-N'-methylenebenzohydrazide derivatives were synthesized. The two compounds 4c and 4g showed an IC50 near the positive control, led to a drastic inhibition of ty-rosinase. Confirming in vitro results were performed via the molecular docking analysis demon-strating hydrogen bound interactions of potent compounds with histatidine-Cu+2 residues with in the active site. Kinetic study of compound 4g showed competitive inhibition towards tyrosinase. Metal chelating assay indicates the mole fraction of 1:2 stoichiometry of the 4g-Cu2+ complex. Conclusion: The findings in the present study demonstrate that 4-Hydroxy-N'-methylenebenzohydrazide scaffold could be regarded as a bioactive core inhibitor of tyrosinase and can be used as an inspiration for further studies in this area.

Synthesis and structure-activity relationship studies of hydrazide-hydrazones as inhibitors of laccase from trametes versicolor

A series of hydrazide-hydrazones 1-3, the imine derivatives of hydrazides and aldehydes bearing benzene rings, were screened as inhibitors of laccase from Trametes versicolor. Laccase is a copper-containing enzyme which inhibition might prevent or reduce the activity of the plant pathogens that produce it in various biochemical processes. The kinetic and molecular modeling studies were performed and for selected compounds, the docking results were discussed. Seven 4-hydroxybenzhydrazide (4-HBAH) derivatives exhibited micromolar activity Ki = 24-674 μM with the predicted and desirable competitive type of inhibition. The structure-activity relationship (SAR) analysis revealed that a slim salicylic aldehyde framework had a pivotal role in stabilization of the molecules near the substrate docking site. Furthermore, the presence of phenyl and bulky tert-butyl substituents in position 3 in salicylic aldehyde fragment favored strong interaction with the substrate-binding pocket in laccase. Both 3- and 4-HBAH derivatives containing larger 3-tert-butyl-5-methyl- or 3,5-di-tert-butyl-2-hydroxy-benzylidene unit, did not bind to the active site of laccase and, interestingly, acted as non-competitive (Ki = 32.0 μM) or uncompetitive (Ki = 17.9 μM) inhibitors, respectively. From the easily available laccase inhibitors only sodium azide, harmful to environment and non-specific, was over 6 times more active than the above compounds.

Thymidine phosphorylase and prostrate cancer cell proliferation inhibitory activities of synthetic 4-hydroxybenzohydrazides: In vitro, kinetic, and in silico studies

Over-expression of thymidine phosphorylase (TP) plays a key role in many pathological complications, including angiogenesis which leads to cancer cells proliferation. Thus in search of new anticancer agents, a series of 4-hydroxybenzohydrazides (1–29) was

Novel hydrazine derivatives having PLK1 inhibition activity and use thereof

The present invention relates to a novel hydrazine derivative having polo-like kinase 1 (PLK1) inhibitory activities, and a use thereof. More specifically, the compound, according to the invention, inhibits activities of PLK1 and suppresses proliferation of cancer cells. Thus, a pharmaceutical composition containing the same as an active ingredient can be useful for preventing or treating cancer.COPYRIGHT KIPO 2018

Antiproliferative and antioxidative effects of novel hydrazone derivatives bearing coumarin and chromene moiety

[InlineMediaObject not available: see fulltext.] A series of new hybrid molecules with a hydrazone fragment were synthesized and characterized by Fourier transform-infrared spectroscopy, nuclear magnetic resonance, mass spectrometry, and elemental analysi

Design, synthesis and in vitro antimalarial activity of an acylhydrazone library

A library of acylhydrazone iron chelators was synthesized and tested for its ability to inhibit the growth of a chloroquine-resistant strain of Plasmodium falciparum. Some of these new compounds are significantly more active than desferrioxamine DFO, the

Synthesis of New Acylhydrazones as Iron-Chelating Compounds

Fourteen acylhydrazides have been condensed with three aromatic o-hydroxy aldehydes (pyridoxal, salicylaldehyde, and 2-hydroxy-1-naphthaldehyde) to give 42 acylhydrazones, of which 38 are new.These compounds complex iron and have shown varying abilities to promote the movement of iron across biological membranes.Their infrared and nuclear magnetic resonance spectra support the structures assigned to them.