5706-76-3

Basic information

• Product Name: 3-nitrobenzaldehyde thiosemicarbazone
• Synonyms: 2-[(3-nitrophenyl)methylene]hydrazine-1-carbothioamide; benzaldehyde, 3-nitro-, 2-[(1Z)-aminomercaptomethylene]hydrazone; hydrazinecarbothioamide, 2-[(3-nitrophenyl)methylene]-, (2E)-; N'-[(E)-(3-nitrophenyl)methylidene]carbamohydrazonothioic acid
• CAS NO: 5706-76-3
• Molecular Formula: C₈H₈N₄O₂S
• Molecular Weight: 224.2397
• Mol File: 5706-76-3.mol
• Article Data: 22

Chemical Properties

• Boiling Point: 397.7°C at 760 mmHg
• Flash Point: 194.3°C
• Density: 1.46g/cm³
• Vapor Pressure: 1.56E-06mmHg at 25°C
• Refractive Index: 1.679
• CAS DataBase Reference: 3-nitrobenzaldehyde thiosemicarbazone(CAS DataBase Reference)
• NIST Chemistry Reference: 3-nitrobenzaldehyde thiosemicarbazone(5706-76-3)
• EPA Substance Registry System: 3-nitrobenzaldehyde thiosemicarbazone(5706-76-3)

Safety Data

• Hazardous Substances Data: 5706-76-3(Hazardous Substances Data)

Upstream product

• 99-61-6 3-nitro-benzaldehyde 
• 79-19-6 thiosemicarbazide 
• 41097-40-9 (E,E)-1,4-bis(3-nitrophenyl)-2,3-diaza-1,3-butadiene 
• 4346-94-5 thiosemicarbazide hydrochloride 

Downstream Products

• 833-47-6 5-(3-nitrophenyl)-1,3,4-thiadiazol-2-amine 
• 7407-92-3 3-amino-benzaldehyde-thiosemicarbazone 
• 134951-66-9 C₂₃H₁₇N₇O₂S 
• 102367-67-9 5-(3-nitro-phenyl)-[1,3,4]thiadiazol-2-ylamine; hydrochloride 
• 137609-10-0 [2-(3-Nitro-phenyl)-4-oxo-thiazolidin-3-yl]-thiourea 
• 119321-43-6 C₁₃H₁₁N₅O₅S*BrH 
• 163555-82-6 C₁₈H₁₁ClN₄O₄S 
• 137609-30-4 5-(3-Nitro-phenyl)-thiazolo[4,3-b][1,3,4]thiadiazol-2-ylamine 

Relevant articles and documents

Synthesis, in vitro thymidine phosphorylase activity and molecular docking study of thiadiazole bearing isatin analogs

A series of seventeen analogs (1─17) were synthesized and characterized through different spectroscopic techniques such as 1H, 13CNMR, HR-EI-MS and were evaluated for in vitro thymidine phosphorylase inhibition. All compounds showed excellent to good thymidine phosphorylase activity having IC50 value ranging between 4.10 ± 0.20 and 54.60 ± 1.40?μM when compared with standard drug 7-deazaxanthine (IC50 = 38.68 ± 1.12?μM). Among the series, compounds 1 (IC50 = 8.30 ± 0.30?μM), 6 (IC50 = 6.30 ± 0.10?μM), 11 (IC50 = 8.40 ± 0.30?μM) and 16 (IC50 = 4.10 ± 0.20?μM) were found more potent. Potent compounds were further subjected to molecular docking study to identify their interactions with the active site of amino acid. Structure activity relationship was done for all analogs mostly based on substitution pattern on phenyl and isatin rings. Graphic abstract: [Figure not available: see fulltext.]

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.

Synthesis, in vitro α-glucosidase inhibitory potential and molecular docking study of thiadiazole analogs

α-Glucosidase is a catabolic enzyme that regulates the body's plasma glucose levels by providing energy sources to maintain healthy functioning. 2-Amino-thiadiazole (1–13) and 2-amino-thiadiazole based Schiff bases (14–22) were synthesized, characterized by 1H NMR and HREI-MS and screened for α-glucosidase inhibitory activity. All twenty-two (22) analogs exhibit varied degree of α-glucosidase inhibitory potential with IC50 values ranging between 2.30 ± 0.1 to 38.30 ± 0.7 μM, when compare with standard drug acarbose having IC50 value of 39.60 ± 0.70 μM. Among the series eight derivatives 1, 2, 6, 7, 14, 17, 19 and 20 showed outstanding α-glucosidase inhibitory potential with IC50 values of 3.30 ± 0.1, 5.80 ± 0.2, 2.30 ± 0.1, 2.70 ± 0.1, 2.30 ± 0.1, 5.50 ± 0.1, 4.70 ± 0.2, and 5.50 ± 0.2 μM respectively, which is many fold better than the standard drug acarbose. The remaining analogs showed good to excellent α-glucosidase inhibition. Structure activity relationship has been established for all compounds. The binding interactions of these compounds were confirmed through molecular docking.