78225-79-3

Upstream product

• 333-20-0 potassium thioacyanate 
• 99-33-2 3,5-dinitrobenoyl chloride 
• 540-72-7 sodium thiocyanide 
• 1147550-11-5 ammonium thiocyanate 
• 99-34-3 3,5-dinitrobenzoic acid 

Downstream Products

• 1139780-29-2 C₁₆H₁₀N₆O₆S 
• 1312990-89-8 1-(4,6-dimethylpyrimidin-2-yl)-3-(3,5-dinitrobenzoyl)thiourea 
• 1454320-43-4 1-(4,6-dimethoxypyrimidin-2-yl)-3-(3,5-dinitrobenzoyl)thiourea 
• 1454320-44-5 1-(4-ethyl-6-methylpyrimidin-2-yl)-3-(3,5-dinitrobenzoyl)thiourea 
• 1454320-45-6 1-(4,6-diethylpyrimidin-2-yl)-3-(3,5-dinitrobenzoyl)thiourea 
• 1454320-46-7 1-(4-ethoxy-6-methoxypyrimidin-2-yl)-3-(3,5-dinitrobenzoyl)thiourea 
• 1454320-47-8 1-(4-methoxy-6-methylpyrimidin-2-yl)-3-(3,5-dinitrobenzoyl)thiourea 
• 1454320-48-9 1-(4-ethoxy-6-ethylpyrimidin-2-yl)-3-(3,5-dinitrobenzoyl)thiourea 
• 1454320-49-0 1-(4,6-diethoxypyrimidin-2-yl)-3-(3,5-dinitrobenzoyl)thiourea 
• 1454320-51-4 N-[(2Z)-3-(4,6-dimethoxypyrimidin-2-yl)-4-phenyl-1,3-thiazol-2(3H)-ylidene]-3,5-dinitrobenzamide 
• 1454320-52-5 N-[(2Z)-3-(4-ethyl-6-methylpyrimidin-2-yl)-4-phenyl-1,3-thiazol-2(3H)-ylidene]-3,5-dinitrobenzamide 
• 1454320-53-6 N-[(2Z)-3-(4,6-diethylpyrimidin-2-yl)-4-phenyl-1,3-thiazol-2(3H)-ylidene]-3,5-dinitrobenzamide 
• 1454320-54-7 N-[(2Z)-3-(4-ethoxy-6-methoxypyrimidin-2-yl)-4-phenyl-1,3-thiazol-2(3H)-ylidene]-3,5-dinitrobenzamide 
• 1454320-55-8 N-[(2Z)-3-(4-methyl-6-methoxypyrimidin-2-yl)-4-phenyl-1,3-thiazol-2(3H)-ylidene]-3,5-dinitrobenzamide 

Relevant academic research and scientific papers

Synthesis of novel acylthioureas bearing naphthoquinone moiety as dual sensor for high-performance naked-eye colorimetric and fluorescence detection of CN? and F? ions and its application in water and food samples

In this study, six new acylthiourea, bearing naphthoquinone moiety, sensors were synthesized in high yield (88–96%) and characterized using 1H/13C NMR, FT-IR and HRMS techniques. All synthesized sensors (4a-f) showed shifts in absorb

Synthesis, computational studies and enzyme inhibitory kinetics of benzothiazole-linked thioureas as mushroom tyrosinase inhibitors

Herein, we report synthesis of a set of benzothiazole-thiourea hybrids with aromatic and aliphatic side chains (BT1 to BT9) using an elegant synthetic strategy. The newly synthesized benzothiazole-thiourea conjugates were subjected to In-vitro tyrosinase inhibition and free radical scavenging activity. Majority of the compounds indicated inhibition considerably improved than the standard; compound (Kojic acid with IC50 = 16.8320 ± 1.1600 μM) BT2 with IC50 = 1.3431 ± 0.0254 μM was found to be the best inhibitor. A non-competitive mode of inhibition of BT2 was disclosed with Ki value of 2.8 μM. In order to study enzyme-inhibitor interactions SAR analysis molecular docking was carried out. The amino groups of thiourea were involved in hydrogen bonding with Glu322 showing the bond length of 1.74 and 2.70 ?, respectively. Moreover, the coupling of π-π was displayed between benzothiazole and benzene rings of His244 and His263, respectively. The outcome of this study might help to develop new inhibitors of melanogenesis, important for cosmetic and food products. Communicated by Ramaswamy H. Sarma.

Preparation, structure determination, and in silico and in vitro Elastase inhibitory properties of substituted N-([1,1′-Biphenyl]-2-ylcarbamothioyl)- Aryl/Alkyl benzamide Derivatives

The preparation of a set of eight closely related biphenyl-thiourea conjugates with aromatic and aliphatic side chains (3a-3h) using a one-pot three-component strategy is reported. All the novel compounds were characterized by spectroscopic techniques (FT

Exploring amantadine derivatives as urease inhibitors: Molecular docking and structure–activity relationship (sar) studies

This article describes the design and synthesis of a series of novel amantadine-thiourea conjugates (3a–j) as Jack bean urease inhibitors. The synthesized hybrids were assayed for their in vitro urease inhibition. Accordingly, N-(adamantan-1-ylcarbamothio

4-aminocoumarin based aroylthioureas as potential jack bean urease inhibitors; synthesis, enzyme inhibitory kinetics and docking studies

Background: Urease enzyme catalyzes the hydrolysis of urea into ammonia and CO2, excess ammonia causes global warming and crop reduction. Ureases are also responsible for certain human diseases such as stomach cancer, peptic ulceration, pyelone

Aroylthiourea derivatives of ciprofloxacin drug as DNA binder: Theoretical, spectroscopic and electrochemical studies along with cytotoxicity assessment

Aroylthiourea derivatives of ciprofloxacin drug — [1-cyclopropyl-6-fluoro-7-(4-((4-methoxybenzoyl)carbamothioyl)piperazin-1-yl)-4-oxo-1,4-dihydroquinoline-3-carboxylic acid] ATU-1, [1-cyclopropyl-7-(4-((2,4-dibromobenzoyl)carbamothioyl)piperazin-1-yl)-6-fluoro-4-oxo-1,4-dihydroquinoline-3-carboxylic acid] ATU-2, and [1-cyclopropyl-7-(4-((3,5-dinitrobenzoyl)carbamothioyl)piperazin-1-yl)-6-fluoro-4-oxo-1,4-dihydroquinoline-3-carboxylic acid] ATU-3 were synthesized, characterized and investigated for DNA binding at stomach pH (4.7) and at 37 °C. All findings by using DFT, molecular docking, spectroscopic (UV-, fluorescence; FL-), cyclic voltammetric (CV) and viscometric techniques revealed that these compounds have the potency to bind with DNA via a mixed mode of interaction. The binding affinity of ATU-1 was evaluated comparatively greater with Kb × 104/M?1 (docking; 5.55, UV-; 7.93, FL-; 5.62, CV; 6.06), ΔG/kJmol?1(docking; ?27.07, UV-; ?29.07, FL-; ?28.18, CV; ?28.38) and n (FL-; 1.20, CV; 2.72). Stern-Volmer quenching constant (Ksv) further pointed towards comparatively greater binding affinity of ATU-1 for DNA, while bimolecular quenching constant (Kq) values showed the involvement of static quenching mechanism in the compound — DNA interaction. Comparatively lesser IC50 (7.1 μM) value obtained from biological work on Huh-7 cancer cell line further confirmed the greater anticancer potential of ATU-1 than that of ATU-2&3.

Synthesis, molecular docking and kinetic studies of novel quinolinyl based acyl thioureas as mushroom tyrosinase inhibitors and free radical scavengers

The enzyme tyrosinase plays a vital role in melanin biosynthesis and enzymatic browning of vegetables and fruits. A series of novel quinolinyl thiourea analogues (11a-j) were synthesized by reaction of 3-aminoquinoline and corresponding isothiocyanates, i

Synthesis and enzyme inhibitory kinetics of some novel 3-(substituted benzoyl)-2-thioxoimidazolidin-4-one derivatives as α-glucosidase/α-amylase inhibitors

The present work describes an efficient and convenient synthesis of a library of novel 3-(substituted benzoyl)-2-thioxoimidazolidin-4-ones (3a–j). The benzoyl isothiocyanates were treated with glycine in the presence of pyridine, the reactants got consumed giving a variety of thioxoimidazolidin-4-ones derivatives under mild reaction conditions. The structures of the compounds were determined by elemental analysis, FTIR, 1H, 13C NMR and mass spectral data. The title compounds were tested for their potential to inhibit the activity of enzymes α-glucosidase and α-amylase. It was found that most of the derivatives showed good enzyme inhibitory activity while compound 3j exhibited excellent activity with IC50 values 0.051 and 0.0082 mM for α-glucosidase and α-amylase, respectively. The presence of 3,5-di-NO2 functional groups at aromatic ring in compound 3j play important role in enzyme inhibitory activity. The enzyme inhibitory kinetic analysis of the most potent derivative 3j revealed that it is a mixed type inhibitor of α-glucosidase with Ki and Ki? values 0.0339 and 0.1562 mM, respectively. It was further investigated that compound 3j formed reversible enzyme inhibitor complex with α-glucosidase. The cytotoxicity of all the synthesized compounds was also evaluated and results showed that none of these compounds displayed toxicity against brine shrimps. Based upon results, it is suggested that compound 3j may act as a lead structure for the development of most potent α-glucosidase inhibitors.

Synthesis, carbonic anhydrase inhibitory activity and antioxidant activity of some 1,3-oxazine derivatives

(Table presented.). A series of 1-(6-methyl-2-substituted phenyl-4-thioxo-4H-1,3-oxazin-5-yl)ethanones (3a-n) were synthesized by the reaction of benzoyl isothiocyanates with active methylene compound acetylacetone in the presence of triethyl amine in a one-pot process. The structures of the products were elucidated by elemental analyses, FT-IR, 1H NMR, 13C NMR, and mass spectroscopy. These new 1,3-oxazine derivatives were evaluated for their inhibitory activity against carbonic anhydrase II. Results for in vitro assay revealed that compound 3b having 4-methoxy phenyl moiety was the most potent inhibitor with IC50 value of 0.144 ± 0.008 μM. It exhibited higher enzyme inhibitory activity as compared to the standard acetazolamide (IC50 = 0.997 ± 0.061 μM). The compounds 3c, 3h, and 3n also displayed superior inhibitory activities compared to the rest of the synthesized oxazine derivatives. The radical scavenging activity of oxazine derivatives was also performed and it was found that compounds showed moderate antioxidant activity. Lipinski rule confirmed the therapeutic potential of the synthesized compounds. Molecular docking studies were also performed to further understand the binding affinity of these compounds with PDBID 1V9E which confirmed that the synthesized derivatives bind in the active binding site of the target protein. Based upon our results, it is proposed that compound 3b may serve as a lead structure to design more potent carbonic anhydrase inhibitors.

Synthesis of sulfadiazinyl acyl/aryl thiourea derivatives as calf intestinal alkaline phosphatase inhibitors, pharmacokinetic properties, lead optimization, Lineweaver-Burk plot evaluation and binding analysis

To seek the new medicinal potential of sulfadiazine drug, the free amino group of sulfadiazine was exploited to obtain acyl/aryl thioureas using simple and straightforward protocol. Acyl/aryl thioureas are well recognized bioactive pharmacophore containin