54191-12-7

Basic information

• Product Name: N-(4-nitrophenyl)butanamide
• Synonyms: N-(4-nitrophenyl)butanamide
• CAS NO: 54191-12-7
• Molecular Formula: C₁₀H₁₂N₂O₃
• Molecular Weight: 208.21388
• Mol File: 54191-12-7.mol

Chemical Properties

• Boiling Point: 417.3°Cat760mmHg
• Flash Point: 206.1°C
• Appearance: /
• Density: 1.244g/cm³
• Vapor Pressure: 3.59E-07mmHg at 25°C
• Refractive Index: 1.588
• CAS DataBase Reference: N-(4-nitrophenyl)butanamide(CAS DataBase Reference)
• NIST Chemistry Reference: N-(4-nitrophenyl)butanamide(54191-12-7)
• EPA Substance Registry System: N-(4-nitrophenyl)butanamide(54191-12-7)

Safety Data

• Hazardous Substances Data: 54191-12-7(Hazardous Substances Data)

Usage

InChI:InChI=1/C10H12N2O3/c1-2-3-10(13)11-8-4-6-9(7-5-8)12(14)15/h4-7H,2-3H2,1H3,(H,11,13)

Upstream product

• 100-01-6 4-nitro-aniline 
• 141-75-3 butyryl chloride 
• 636-98-6 p-nitrobenzene iodide 
• 541-35-5 butanamide 
• 133-13-1 ethyl diethyl malonate 
• 106-31-0 butanoic acid anhydride 

Downstream Products

• 100-01-6 4-nitro-aniline 
• 109817-62-1 1-(4'-aminophenyl)-5-propyl-1H-tetrazole 
• 1596358-22-3 1-(4'-nitrophenyl)-5-propyl-1H-tetrazole 
• 58259-34-0 N-butyl-4-nitroaniline 
• 116884-02-7 butyric acid-(4-amino-anilide) 

Relevant articles and documents

Phenanthridin-6-one derivatives as the first class of non-steroidal pharmacological chaperones for Niemann-Pick disease type C1 protein

Niemann-Pick disease type C is a fatal, progressive neurodegenerative disease mostly caused by mutations in Nieamnn-Pick type C1 (NPC1), a late endosomal membrane protein that is essential for intracellular cholesterol transport. The most prevalent mutation, I1061T (Ile to Thr), interferes with the protein folding process. Consequently, mutated but intrinsically functional NPC1 proteins are prematurely degraded via proteasome, leading to loss of NPC1 function. Previously, we reported sterol derivatives as pharmacological chaperones for NPC1, and showed that these derivatives can normalize folding-defective phenotypes of I1061T NPC1 mutant by directly binding to, and stabilizing, the protein. Here, we report a series of compounds containing a phenanthridin-6-one scaffold as the first class of non-steroidal pharmacological chaperones for NPC1. We also examined their structure-activity relationships.

Synthesis and methemoglobinemia-inducing properties of benzocaine isosteres designed as humane rodenticides

A number of isosteres (oxadiazoles, thiadiazoles, tetrazoles and diazines) of benzocaine were prepared and evaluated for their capacity to induce methemoglobinemia - with a view to their possible application as humane pest control agents. It was found that an optimal lipophilicity for the formation of methemoglobin (metHb) in vitro existed within each series, with 1,2,4-oxadiazole 3 (metHb% = 61.0 ± 3.6) and 1,3,4-oxadiazole 10 (metHb% = 52.4 ± 0.9) demonstrating the greatest activity. Of the 5 candidates (compounds 3, 10, 11, 13 and 23) evaluated in vivo, failure to induce a lethal end-point at doses of 120 mg/kg was observed in all cases. Inadequate metabolic stability, particularly towards hepatic enzymes such as the CYPs, was postulated as one reason for their failure.

Malonic ester amide synthesis: An efficient methodology for synthesis of amides

A general methodology malonic ester amide synthesis has been demonstrated, which uses α-substituted/unsubstituted diethyl malonates for the decarboxylative acylation of various aromatic/heteroaromatic primary/secondary amines to form one-carbon homologated amides, thus providing easy access to amides with odd/even chain lengths and an array of substituents on the alkyl/aryl part while avoiding use of acyl chlorides or peptide coupling reagents. Copyright

Iron-catalyzed N-arylations of amides

A method was proposed for iron-catalyzed N-arylation of primary amides and its applicability to the synthesis of N-heterocycles by intramolecular ring closures. The method used a catalyst system of 10 mol % of FeCl3 and 20 mol % of N,N'-dimethylethylenediamine (DMEDA). The study found that secondary amides of N-methylbenzamide and N-benzylbenzamide produce N-arylated products in trace amounts. The method developed an iron-based catalyst system for efficient N-arylations of primary amides with aryl iodides. The study used a sealable tube equipped with a magnetic stir bar charged with amide, or K 3PO4, or K2CO3, or FeCl3. The study used NMR spectroscopic analysis to determine the identity and purity of the products. The method observed that different substituted aryl iodides made a positive impact on the reaction.

Novel retinoid derivatives and methods for producing said compounds and anti-cancer pharmaceutical composition comprising said compounds

The present invention relates to a novel retinoid derivative compound represented by the formula I: wherein X, R1, R2 and R3 are as defined herein or pharmaceutically acceptalbe salts thereof. Also, the present invention relates to processes for producing the compound of the formula I and to an anti-cancer composition comprising the compound of the formula I. The compound of the formula I according to the present invention exerts high anti-cancer effects while not causing undesirable side effects.

Bis(salicylaldehyde)ethylenedi-iminecobalt(II)-catalysed Oxidation of Aromatic Amins with Oxygen

N-n-Butylanilines undergo N-dealkylation to give a primary amine and butyrylaldehyde by oxidation with oxygen in the presence of bis(salicylaldehyde)ethylenedi-iminecobalt(II) (CoIIsalen) as a catalyst.High conversions are obtained with high catalyst concentrations and low / ratios (r).Inspection of the effect of catalyst and substrate concentrations on initial reaction rates (Vin) shows poor sensitivity to the electronic effect of the nuclear substituent.Some anilines give azo derivatives at a lower rate in the same conditions.

p-Nitroanilides of 3-carboxypropionyl-peptides. Their cleavage by elastase, trypsin, and chymotrypsin.

Fourteen 3-carboxypropionyl-tripeptide-p-nitroanilides of the general formula 3-carboxypropionyl-alanyl-alanyl-Y-p-nitroanilide (Y = glycine, norvaline, S-methylcysteine, valine, norleucine, S-ethylcysteine, methionine, leucine, isoleucine, phenylalanine, tyrosine, S-benzylcysteine, Calpha-phenylglycine, and proline) were synthesized and their cleavage by elastase, trypsin, and chymotrypsin (Km, kcat and kcat/Km) was determined. The significance of amino acid residues in the position of Y was evaluated firstly with respect to their structure (topographically), and secondly with respect to their free energy (thermodynamically). The alanine residue substrate was cleaved best by elastase, the phenylalanine substrate by chymotrypsin. Trypsin cleaved two substrates only, that is those containing a phenylalanine and a tyrosine residue. The optimum length of the elastolytic substrates was studied in a series of N-3-carboxypropionyl-(Ala)n-p-nitroanilides (n = 1, 2, 3, 4, 5), N-3-carboxypropionyl-(Gly)n-p-nitroanilides (n = 1, 2, 3), and in p-nitroanilides of fatty acids with two to seven carbon atoms. Elastase cleaved tri, tetra, and pentapeptides of alanine. p-Nitroanilides of the glycine series, as well as p-nitroanilides of fatty acids were not cleaved. 3-Carboxypropionyl-tetra-alanine-p-nitroanilide was the most suitable substrate so far found for elastase cleavage; it is not cleaved by trypsin nor chymotrypsin. The optimum distance between Y and the terminal anionic carboxyl residue was found to be 1.8 nm in elastolytic substrates.