779-30-6

Basic information

• Product Name: 3-ACETAMIDOCOUMARIN
• Synonyms: 3-(AcetylaMino)couMarin;N-(2-Oxo-2H-1-benzopyran-3-yl)acetaMide;NSC 65873;3-ACETAMIDOCOUMARIN;ACETAMIDOCOUMARIN, 3-;N-(2-Oxo-2H-chromen-3-yl)acetamide;3-ACETAMIDOCOUMARIN 99%;PALMATINE CHLORIDE(P)
• CAS NO: 779-30-6
• Molecular Formula: C₁₁H₉NO₃
• Molecular Weight: 203.19
• EINECS: 125-784-9
• Product Categories: Aromatics;Intermediates & Fine Chemicals;Pharmaceuticals;Coumarin;Building Blocks;Coumarins;Heterocyclic Building Blocks;Amines
• Mol File: 779-30-6.mol

Chemical Properties

• Melting Point: 205-207 °C(lit.)
• Boiling Point: 482 °C at 760 mmHg
• Flash Point: 245.3 °C
• Appearance: /
• Density: 1.31 g/cm³
• Vapor Pressure: 1.89E-09mmHg at 25°C
• Refractive Index: 1.604
• CAS DataBase Reference: 3-ACETAMIDOCOUMARIN(CAS DataBase Reference)
• NIST Chemistry Reference: 3-ACETAMIDOCOUMARIN(779-30-6)
• EPA Substance Registry System: 3-ACETAMIDOCOUMARIN(779-30-6)

Safety Data

• Safety Statements: S22:Do not inhale dust.; S24/25:Avoid contact with skin and eyes.
• WGK Germany: 3
• Hazardous Substances Data: 779-30-6(Hazardous Substances Data)

Usage

Uses

Used in Analytical Chemistry:
3-ACETAMIDOCOUMARIN is used as a matrix in MALDI TOF-MS (Matrix-Assisted Laser Desorption/Ionization Time-of-Flight Mass Spectrometry) analysis for polyethylene glycol (PEG) samples. Its role as a matrix is crucial in this technique, as it helps in the ionization and desorption of the analyte molecules, facilitating their detection and analysis. The antioxidant activity of 3-ACETAMIDOCOUMARIN contributes to its stability and effectiveness in this application.
Used in Pharmaceutical Research:
Due to its unique chemical structure and antioxidant properties, 3-ACETAMIDOCOUMARIN holds potential in the development of new pharmaceutical compounds. It can be used as a starting material or a building block for the synthesis of more complex molecules with therapeutic applications. Researchers can explore its potential in various areas, such as anti-inflammatory, antimicrobial, or anticancer drugs, by modifying its structure and evaluating its biological activities.

InChI:InChI=1/C11H9NO3/c1-7(13)12-9-6-8-4-2-3-5-10(8)15-11(9)14/h2-6H,1H3,(H,12,13)

Upstream product

• 24474-93-9 2-methyl-4H-oxazol-5-one 
• 90-02-8 salicylaldehyde 
• 543-24-8 N-acetylglycine 
• 91137-46-1 3-(1-hydroxyimino-ethyl)-coumarin 
• 10026-13-8 phosphorus pentachloride 
• 7719-12-2 phosphorus trichloride 
• 60-35-5 acetamide 
• 939-18-4 3-bromo-2H-chromen-2-one 
• 1635-31-0 aminocoumarine 
• 75-36-5 acetyl chloride 
• 1906-82-7 ethyl acetamidoacetate 
• 3949-36-8 3-acetylcoumarin 

Downstream Products

• 1635-31-0 aminocoumarine 
• 5818-89-3 Chromannedione-2,3 
• 6803-09-4 3-(2'-hydroxyphenyl)-2-hydroxypropanoic acid 
• 709-16-0 2-hydroxy-phenylalanine 
• 939-19-5 3-Hydroxy-cumarin 
• 1473-60-5 3-[(2-hydroxy-benzylidene)amino]chromen-2-one 
• 144616-79-5 3-{[1-Phenyl-meth-(E)-ylidene]-amino}-chromen-2-one 
• 178909-14-3 3-{[1-(3,4-Dimethoxy-phenyl)-meth-(E)-ylidene]-amino}-chromen-2-one 
• 119824-81-6 1,3-diphenyl-4-oxo-3H-benzopyrano<3,4-c>pyrazole 
• 112517-42-7 3-{[1-(4-Dimethylamino-phenyl)-meth-(E)-ylidene]-amino}-chromen-2-one 
• 112517-49-4 C₂₀H₁₃N₃O₃ 
• 112517-44-9 C₂₂H₁₅N₃O₃ 
• 112517-50-7 C₂₀H₁₃N₃O₄ 
• 112517-51-8 C₂₄H₂₀N₄O₂ 

Relevant articles and documents

A convenient and expeditious synthesis of 3-(N-substituted) aminocoumarins via palladium-catalyzed Buchwald-Hartwig coupling reaction

A convenient protocol for the rapid and efficient synthesis of 3-(N-substituted) aminocoumarins is described. The synthetic route developed involves the Pd-catalyzed C-N coupling reaction from readily available 3-bromocoumarin derivatives in the presence of the catalytic system Pd(OAc)2/Xantphos. Under these conditions, a series of nucleophiles including amides, sulfonamides, carbamates and functionalized amines, have been successfully reacted to afford the coupling products in fair to good yields.

Design, synthesis and biological evaluation of selective hybrid coumarin-thiazolidinedione aldose reductase-II inhibitors as potential antidiabetics

Thiazolidinediones (TZD), benzopyrans are the proven scaffolds for inhibiting Aldose reductase (ALR2) activity and their structural confluence with the retention of necessary fragments helped in designing a series of hybrid compounds 2-(5-cycloalkylidene-2,4-dioxothiazolidin-3-yl)-N-(2-oxo-2H-chromen-3-yl)acetamide (10a-n) for better ALR2 inhibition. The compounds were synthesized by treating substituted 3-(N-bromoacetyl amino)coumarins (9a-d) with potassium salt of 5-cyclo alkylidene-1,3-thiazolidine-2,4-diones (4a-d). The inhibition activity against ALR2 with IC50 values range from 0.012 ± 0.001 to 0.056 ± 0.007 μM. N-[(6-Bromo-3-coumarinyl)-2-(5-cyclopentylidene-2,4-dioxothiazolidin-3-yl)] acetamide (10c) with cyclopentylidene group on one end and the 6-bromo group on the other end showed better inhibitory property (IC50 = 0.012 μM) and selectivity index (324.166) against the ALR2, a forty fold superiority over sorbinil, a better molecule over epalrestat and rest of the analogues exhibited a far superior response over sorbinil and slightly better as compared with epalrestat. It was further confirmed by the insilico studies that compound 10c showed best inhibition activity among the synthesized compounds with a high selectivity index against the ALR2. In invivo experiments, supplementation of compound 10c to STZ induced rats delayed the progression of cataract in a dose-dependent manner warranting its further development as a potential agent to treat the diabetic secondary complications especially cataract.

Mild and highly efficient deacetylation of acetamido and acetoxy coumarins: A convenient and expeditious synthesis of substituted 3-aminocoumarins

A convenient protocol for efficient and cost-effective method for synthesis of substituted 3-aminocoumarins has been developed. The synthetic route involves expeditious and fast quantitative deacetylation of readily available acetamido derivative under anhydrous acidic conditions, employing thionyl chloride in methanol, without formation of undesired substituted 3-hydroxycoumarins. The method is suitable for derivatives bearing electron-donating as well as electron-withdrawing groups at position 7 of the coumarin scaffold. Under these conditions, a series of acetoxy substituted 3-dialkylaminocoumarins has been also successfully deacetylated to afford easily isolable corresponding hydroxy derivatives in high yields.

Beckmann rearrangement: Thiamine hydrochloride as a remarkable catalyst for one-pot synthesis of amides from ketones

Thiamine hydrochloride catalyzed synthesis of amides from ketones including 3-acetyl coumarin via Beckmann rearrangement has been reported. The reaction is believed to involve oxime formation, cleavage of C[sbnd]C bond followed by C[sbnd]N bond formation in one-pot. Thiamine hydrochloride is stable, cheap, easy to handle and environmentally friendly.

Rational design, synthesis and biological evaluation of novel multitargeting anti-AD iron chelators with potent MAO-B inhibitory and antioxidant activity

A series of (3-hydroxypyridin-4-one)-coumarin hybrids were developed and investigated as potential multitargeting candidates for the treatment of Alzheimer's disease (AD) through the incorporation of iron-chelating and monoamine oxidase B (MAO-B) inhibition. This combination endowed the hybrids with good capacity to inhibit MAO-B as well as excellent iron-chelating effects. The pFe3+ values of the compounds were ranging from 16.91 to 20.16, comparable to more potent than the reference drug deferiprone (DFP). Among them, compound 18d exhibited the most promising activity against MAO-B, with an IC50 value of 87.9 nM. Moreover, compound 18d exerted favorable antioxidant activity, significantly reversed the amyloid-β1-42 (Aβ1-42) induced PC12 cell damage. More importantly, 18d remarkably ameliorated the cognitive dysfunction in a scopolamine-induced mice AD model. In brief, a series of hybrids with potential anti-AD effect were successfully obtained, indicating that the design of iron chelators with MAO-B inhibitory and antioxidant activities is an attractive strategy against AD progression.

Evaluation of novel coumarin-proline sulfonamide hybrids as anticancer and antidiabetic agents

Cancer and diabetes are considered as two major diseases affecting human health worldwide. Various therapies are available for treatment of cancer and diabetes individually, peptide linkage containing proline sulfonamide can be a promising therapy for treatment of both cancer as well as diabetes. Here, we report design and synthesis of novel coumarin-proline sulfonamide derivatives as anticancer and antidiabetic agents. All the synthesized compounds were screened for their anticancer activity against lungs cancer cell line (A549) and breast cancer cell line (MCF7) using 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide dye (MTT)assay and antidiabetic activity using DPP-IV inhibition assay. Compound 16b showed excellent activity against breast cancer cell line (MCF7) with IC50 value of 1.07 μM. All compounds showed moderate DPP-IV inhibition.

Evaluation of trypanocidal and antioxidant activities of a selected series of 3-amidocoumarins

Background: Neglected diseases are becoming more prevalent due to globalization. This has inspired active research in the development of new drugs for the treatment of parasitic diseases such as Chagas disease. Objectives: With the aim of finding new tryp

Design and synthesis of aminocoumarin derivatives as DPP-IV inhibitors and anticancer agents

DPP-IV “a moonlighting protein” has immerged as promising pathway to control Type 2 diabetes as well as found to play key role in earlier stages of cancer. Here we have reported design, synthesis and applications of aminocoumarin derivatives as DPP-IV inhibitors. Compounds have been synthesized and studied for their DPP-IV inhibition activity. Three compounds have shown moderate inhibition at 100 μM concentration. All compounds were also screened for their anticancer activity against A549 (Lung cancer cell line), MCF-7 (Breast cancer cell line) using MTT assay. One of the compounds has shown very good anticancer activity with IC50 value 24 ± 0.1 nM against A549 cell line.

A novel class of human 15-LOX-1 inhibitors based on 3-hydroxycoumarin

Inflammations, sensitivities, and some cancers in mammals are intimately linked to the activity of lipo-oxygenase enzymes. Owing to the importance of these enzymes, mechanistic studies, product analysis, and synthesis of inhibitors have expanded. In this study, a series of hydroxycoumarins, methoxy-3-hydroxy coumarins, and 7-alkoxy-3-hydroxy coumarins were synthesized and evaluated as potential inhibitors of human 15-LOX-1. Among the synthetic coumarins, 7-methoxy-3-hydroxycoumarin derivative demonstrated potent inhibitory activity and the compound, 5f, showed the best result. Radical scavenging assessment, IC50, HNMR, and DPPH bleaching results indicate that the electronic properties are the major factors for the lipo-oxygenase inhibition potency of the synthetic coumarins. Based on the theoretical studies, it was suggested that the mesomeric effect of the substituent at the seventh position of the benzene ring is one of the major factors in the stability of the oxy-radical intermediate.

Synthesis of 3-aminocoumarin-N-benzylpyridinium conjugates with nanomolar inhibitory activity against acetylcholinesterase

A series of 3-amino-6,7-dimethoxycoumarins conjugated with the N-benzylpyridinium moiety through an amide-bond linkage was synthesized and evaluated for their acetylcholinesterase inhibitory activity. A number of the benzylpyridinium derivatives exhibited potent activities with inhibitory concentration (IC50) values in the nanomolar concentration range. Among them, the 2,3-difluo-robenzylpyridinium-containing compound was the most potent inhibitor with an IC50 value of 1.53 ± 0.01 nM. Docking studies revealed that the synthesized compounds inhibit the target enzyme by a dual binding site mechanism whereby the coumarin portion binds with the peripheral anionic site while the N-benzylpyridinium residue binds with the catalytic anionic site of the enzyme.