2302-93-4

Basic information

• Product Name: Acetophenone thiosemicarbazone
• Synonyms: Acetophenone thiosemicarbazone;acetophenone thiosemicarbazide;1-(α-Methylbenzylidene)thiosemicarbazide;1-Phenylethanone thiosemicarbazone;α-Methylbenzaldehyde thiosemicarbazone
• CAS NO: 2302-93-4
• Molecular Formula: C₉H₁₁N₃S
• Molecular Weight: 193.29
• Mol File: 2302-93-4.mol
• Article Data: 36

Chemical Properties

• Boiling Point: 322.7°Cat760mmHg
• Flash Point: 148.9°C
• Appearance: /
• Density: 1.1549 (rough estimate)
• Vapor Pressure: 0.000275mmHg at 25°C
• Refractive Index: 1.5300 (estimate)
• CAS DataBase Reference: Acetophenone thiosemicarbazone(CAS DataBase Reference)
• NIST Chemistry Reference: Acetophenone thiosemicarbazone(2302-93-4)
• EPA Substance Registry System: Acetophenone thiosemicarbazone(2302-93-4)

Safety Data

• Hazardous Substances Data: 2302-93-4(Hazardous Substances Data)

Usage

Safety Profile

Poison by ingestion andintravenous routes. When heated to decomposition it emitsvery toxic fumes of NOx and SOx.

InChI:InChI=1/C9H11N3S/c1-7(11-12-9(10)13)8-5-3-2-4-6-8/h2-6H,1H3,(H3,10,12,13)/b11-7+

Upstream product

• 56587-83-8 acetophenone azine 
• 79-19-6 thiosemicarbazide 
• 98-86-2 acetophenone 
• 4346-94-5 thiosemicarbazide hydrochloride 

Downstream Products

• 5213-42-3 [4-oxo-2-(1-phenyl-ethylidenehydrazono)-thiazolidin-5-yl]-acetic acid 
• 115163-95-6 thiazolidine-2,4-dione-2-(1-phenyl-ethylLiDenehydrazone) 
• 21198-20-9 2-(1-phenylethyl)hydrazinecarbothioamide 
• 79-19-6 thiosemicarbazide 
• 583-11-9 N-(1-phenylethylidene)phenylhydrazine 
• 22067-32-9 N-(1-phenyl-ethylidene)-N'-(4-phenyl-thiazol-2-yl)hydrazine 
• 109821-31-0 N,N'''-bis-(1-phenyl-ethylidene)-μ-disulfido-dicarboxamidrazone 
• 36937-55-0 1-phenyl-ethanone (4-naphthalen-2-yl-thiazol-2-yl)-hydrazone 
• 69170-40-7 1-phenyl-ethanone [4-(1-methyl-1H-benzoimidazol-2-yl)-thiazol-2-yl]-hydrazone 
• 78938-21-3 S-Benzylisoacetophenonethiosemicarbazone 
• 106467-58-7 5-[3-(4-Methoxy-phenyl)-ureido]-2-methyl-2-phenyl-[1,3,4]thiadiazole-3-carboxylic acid (4-methoxy-phenyl)-amide 

Relevant articles and documents

Organometallic ruthenium(II) complexes containing NS donor Schiff bases: Synthesis, structure, electrochemistry, DNA/BSA binding, DNA cleavage, radical scavenging and antibacterial activities

Four new cyclopentadienylruthenium(II)-acetophenone-4(N)-substituted thiosemi-carbazone complexes, with the general formula [Ru(?5-C5H5)(H-Aptsc)PPh3].Cl (1), [Ru(?5-C5H5)(H-Apmt

Synthesis, characterization, alkaline phosphatase inhibition assay and molecular modeling studies of 1-benzylidene-2-(4-tert- butylthiazol-2-yl) hydrazines

Alkaline phosphatases are homodimeric protein enzymes which removes phosphates from several types of molecules. These catalyze the hydrolysis of monoesters in phosphoric acid which in turn catalyze a transphosphorylation reaction. Thiazoles are a privileged class of heterocyclic compounds which may potentially serve as effective phosphatase inhibitors. In this regard, the present research paper reports the facile synthesis and characterization of substituted 1-benzylidene-2-(4-tert-butylthiazol-2-yl) hydrazines with excellent yields. The synthesized compounds were tested for inhibitory potential against alkaline phosphatases. The compound 1-(4-Hydroxy, 3-methoxybenzylidene)-2-(4-tert-butylthiazol-2-yl) hydrazine (5e) was found to be the most potent inhibitor of human tissue non-alkaline phosphatase in this group of molecules with an IC50 value of 1.09 ± 0.18 μM. The compound 1-(3,4-dimethoxybenzylidene)-2-(4-tert-butylthiazol-2-yl) hydrazine (5d) exhibited selectivity and potency for human intestinal alkaline phosphatase with an IC50 value of 0.71 ± 0.02 μM. In addition, structure activity relationship and molecular docking studies were performed to evaluate their binding modes with the target site of alkaline phosphatase. The docking analysis revealed that the most active inhibitors showed the important interactions within the binding pockets of human intestinal alkaline phosphatase and human tissue non-alkaline phosphatase and may be responsible for the inhibitory activity of the compound towards the enzymes. Therefore, the screened thiazole derivatives provided an outstanding platform for further development of alkaline phosphatase inhibitors.

Combined theoretical and experimental studies reveal the newly synthesized pyrimidinones as potential apoptotic agents

Reaction of acetophenone thiosemicarbazones (5–8) and (2-methyl) diethyl malonate in absolute ethanol under reflux conditions furnished the corresponding pyrimidinone analogs (9–12) in good to excellent yields. The resulting pyrimidines were characterised

Synthesis, characterization, in vitro tissue-nonspecific alkaline phosphatase (TNAP) and intestinal alkaline phosphatase (IAP) inhibition studies and computational evaluation of novel thiazole derivatives

Alkaline phosphatases (APs) are a class of homodimeric enzymes which physiologically possess the dephosphorylation ability. APs catalyzes the hydrolysis of monoesters into phosphoric acid which in turn catalyze a transphosphorylation reaction. Thiazoles are nitrogen and sulfur containing aromatic heterocycles considered as effective APs inhibitors. In this context, the current research paper presents the successful synthesis, spectroscopic characterization and in vitro alkaline phosphatase inhibitory potential of new thiazole derivatives. The structure activity relationship and molecular docking studies were performed to find out the binding modes of the screened compounds with the target site of tissue non-specific alkaline phosphatase (h-TNAP) as well as intestinal alkaline phosphatase (h-IAP). Compound 5e was found to be potent inhibitor of h-TNAP with IC50 value of 0.17 ± 0.01 μM. Additionally, compounds 5a and 5i were found to be highly selective toward h-TNAP with IC50 values of 0.25 ± 0.01 μM and 0.21 ± 0.02 μM, respectively. In case of h-IAP compound 5f was the most potent inhibitor with IC50 value of 1.33 ± 0.10 μM. The most active compounds were resort to molecular docking studies on h-TNAP and h-IAP to explore the possible binding interactions of enzyme-ligand complexes. Molecular dynamic simulations were carried out to investigate the overall stability of protein in apo and holo state.