1489265-34-0

Basic information

• Product Name: (2E)-2-[(2-nitrophenyl)methylidene]hydrazine-1-carbothioamide
• Synonyms: (2E)-2-[(2-nitrophenyl)methylidene]hydrazine-1-carbothioamide
• CAS NO: 1489265-34-0
• Molecular Weight: 224.243
• Mol File: 1489265-34-0.mol

Chemical Properties

• CAS DataBase Reference: (2E)-2-[(2-nitrophenyl)methylidene]hydrazine-1-carbothioamide(CAS DataBase Reference)
• NIST Chemistry Reference: (2E)-2-[(2-nitrophenyl)methylidene]hydrazine-1-carbothioamide(1489265-34-0)
• EPA Substance Registry System: (2E)-2-[(2-nitrophenyl)methylidene]hydrazine-1-carbothioamide(1489265-34-0)

Safety Data

• Hazardous Substances Data: 1489265-34-0(Hazardous Substances Data)

Upstream product

• 4346-94-5 thiosemicarbazide hydrochloride 
• 552-89-6 2-nitro-benzaldehyde 
• 79-19-6 thiosemicarbazide 

Downstream Products

• 832-79-1 5-(2-nitrophenyl)-1,3,4-thiadiazol-2-amine 
• 93691-32-8 (E)-2-((E)-(2-nitrobenzylidene)hydrazono)thiazolidin-4-one 
• 1489265-15-7 ethyl 4-methyl-2-[(E)-2-[(2-nitrophenyl)methylidene]hydrazin-1-yl]-1,3-thiazole-5-carboxylate 

Relevant articles and documents

Aryl thiosemicarbazones for the treatment of trypanosomatidic infections

Basing on a library of thiadiazole derivatives showing anti-trypanosomatidic activity, we have considered the thiadiazoles opened forms and reaction intermediates, thiosemicarbazones, as compounds of interest for phenotypic screening against Trypanosoma b

A Series of Benzylidenes Linked to Hydrazine-1-carbothioamide as Tyrosinase Inhibitors: Synthesis, Biological Evaluation and Structure?Activity Relationship

Tyrosinase is a type 3 copper enzyme responsible for skin pigmentation disorders, skin cancer, and enzymatic browning of vegetables and fruits. In the present article, 12 small molecules of 2-benzylidenehydrazine-1-carbothioamide were designed, synthesized and evaluated for their anti-tyrosinase activities followed by molecular docking and pharmacophore-based screening. Among synthesized thiosemicarbazone derivatives, one compound, (2E)-2-[(4-nitrophenyl)methylidene]hydrazine-1-carbothioamide, is the strongest inhibitor of mushroom tyrosinase with IC50 of 0.05 μM which demonstrated a 128-fold increase in potency compared to the positive control. Kinetic studies also revealed mix type inhibition by this compound. Docking studies confirmed the complete fitting of the synthesized compounds into the tyrosinase active site. The results underline the potential of 2-benzylidenehydrazine-1-carbothioamides as potent pharmacophore to extend the tyrosinase inhibition in drug discovery.

New biologically dynamic hybrid pharmacophore triazinoindole-based-thiadiazole as potent α-glucosidase inhibitors: In vitro and in silico study

Triazinoindole bearing thiadiazole derivatives (1–25) have been synthesized and characterized through different spectroscopic techniques such as 1H, 13C-NMR and HREI-MS. The purpose of the study was to investigate the anti-diabetic activity of the synthesized triazinoindole bearing thiadiazole derivatives by inhibition of α-glucosidase. All synthesized analogues showed outstanding inhibition of α-glucosidase enzyme with IC50 values ranging from 2.5 ± 0.10 to 38.10 ± 0.10 μM as compared to the standard drug acarbose (IC50 = 38.45 ± 0.80 μM). Analogue 4 (IC50 = 2.5 ± 0.10 μM) was identifies as the most potent analogue in the series with fifteen folds more active than standard acarbose. Structure activity relationship (SAR) studies suggested that α-glucosidase activities of triazinoindole bearing thiadiazole are primarily dependent upon on number and position of different substitutions present on phenyl parts. Molecular docking study were conducted of the optimized compounds (i.e., compound 4, 6, and 3 etc. using MOE default parameters), the results revealed that compound 4, 6, and 3 showed numerous key interactions with the target protein, which indicate the high potential of these compounds against the target compound. All these compounds were screened for cytotoxic activity against normal normal Vero cell line and found non-toxic.

Aryl hydrazones linked thiazolyl coumarin hybrids as potential urease inhibitors

Aryl hydrazones bearing thiazolyl coumarin hybrids 1–32 were prepared by following 'one-pot' two-steps reaction scheme. Various arylaldehydes were reacted to thiosemicarbazide under acidic condition to form aryl thiosemicarbazone intermediates which in turn treated with 3-bromoacetyl coumarin under basic condition to afford thiazolyl coumarin hybrids 1–32. All hybrids were recognized by EI- and HREI-MS and 1H- and 13C-NMR spectroscopic techniques. Compounds 1–32 were screened for in vitro inhibitory activity against urease enzyme and displayed good to moderate inhibitory potential in the ranges of IC50 = 16.29 ± 1.1–256.30 ± 1.4?μM. Worth stating that compound 21 (IC50 = 16.29 ± 1.1?μM) was identified as more potent urease inhibitor than the standard acetohydroxamic acid (IC50 = 27.0 ± 0.5?μM). Derivatives 19 (IC50 = 77.67 ± 1.5?μM) and 30 (IC50 = 71.21 ± 1.6?μM) were found to be moderately active. Structure–activity relationship revealed that -F, -Cl, -OH, and -OMe groups and their respective positions on aryl ring are playing important role in urease enzyme inhibition. Molecular docking studies identified important interaction between the ligand (active hybrids) and urease active site.

4-(3-Nitrophenyl)thiazol-2-ylhydrazone derivatives as antioxidants and selective hMAO-B inhibitors: synthesis, biological activity and computational analysis

A new series of 4-(3-nitrophenyl)thiazol-2-ylhydrazone derivatives were designed, synthesised, and evaluated to assess their inhibitory effect on the human monoamine oxidase (hMAO) A and B isoforms. Different (un)substituted (hetero)aromatic substituents were linked to N1 of the hydrazone in order to establish robust structure–activity relationships. The results of the biological testing demonstrated that the presence of the hydrazothiazole nucleus bearing at C4 a phenyl ring functionalised at the meta position with a nitro group represents an important pharmacophoric feature to obtain selective and reversible human MAO-B inhibition for the treatment of neurodegenerative disorders. In addition, the most potent and selective MAO-B inhibitors were evaluated in silico as potential cholinesterase (AChE/BuChE) inhibitors and in vitro for antioxidant activities. The results obtained from molecular modelling studies provided insight into the multiple interactions and structural requirements for the reported MAO inhibitory properties.

Design, Synthesis, and Evaluation of 3-((4-(t-Butyl)-2-(2-benzylidenehydrazinyl)thiazol-5-yl)methyl)quinolin-2(1H)-ones as Neuraminidase Inhibitors

A series of novel 3-((4-(t-butyl)-2-(2-benzylidenehydrazinyl)thiazol-5-yl)methyl)quinolin-2(1H)-ones (7a-7z) were designed, synthesized and evaluated for their ability of inhibiting neuraminidase (NA) of in?uenza H1N1 virus. Some compounds displayed moder

Synthesis, in vitro evaluation and molecular docking studies of thiazole derivatives as new inhibitors of α-glucosidase

A series of thiazole derivatives 1-21 were prepared, characterized by EI-MS and 1H NMR and evaluated for α-glucosidase inhibitory potential. All twenty one derivatives showed good α-glucosidase inhibitory activity with IC50 value ran

Synthesis of 4-thiazolidinone analogs as potent in vitro anti-urease agents

4-Thiazolidinone analogs 1-20 were synthesized, characterized by 1H NMR and EI-MS and investigated for urease inhibitory activity. All twenty (20) analogs exhibited varied degree of urease inhibitory potential with IC50 values 1.73-69.65 μM, if compared with standard thiourea having IC50 value of 21.25 ± 0.15 μM. Among the series, eight derivatives 3, 6, 8, 10, 15, 17, 19, and 20 showed outstanding urease inhibitory potential with IC50 values of 9.34 ± 0.02, 14.62 ± 0.03, 8.43 ± 0.01, 7.3 ± 0.04, 2.31 ± 0.002, 5.75 ± 0.003, 8.81 ± 0.005, and 1.73 ± 0.001 μM, respectively, which is better than the standard thiourea. The remaining analogs showed good to excellent urease inhibition. The binding interactions of these compounds were confirmed through molecular docking studies.

2-(2-Hydrazinyl)thiazole derivatives: Design, synthesis and in vitro antimycobacterial studies

In an attempt to discover new potent inhibitors for Mycobacterium tuberculosis (Mtb), a series of 2-(2-hydrazinyl)thiazole derivatives with a wide range of substitutions at 2-, 4- and 5-positions were designed by considering Lipinski rule. The designed compounds were synthesized, characterized and evaluated for their inhibitory potential against Mtb, H37Rv, by in vitro assay. The compounds, ethyl-4-methyl-2-[(E)-2-[1-(pyridin-2-yl)ethylidene] hydrazin-1-yl]-1,3-thiazole-5-carboxylate, 4d, and ethyl-2-[(E)-2-[(2- hydroxyphenyl)methylidene]hydrazin-1-yl]-4-methyl-1,3-thiazole-5-carboxylate, 2i showed noticeable inhibitory activity against Mtb, H37Rv with minimum inhibitory concentration (MIC) of 12.5 μM and 25 μM respectively. An attempt has been made to understand the mechanism of action by binding interactions of these molecules with β-ketoacyl-ACP synthase protein through docking studies. The inhibition constants for compounds 4d and 2i were found to be 1.46 μM and 0.177 μM respectively.