79127-41-6

Upstream product

• 92642-17-6 N-(5-acetyl-2-nitrophenyl)acetamide 
• 99-03-6 1-(3-aminophenyl)ethanone 
• 7463-31-2 3-Acetamidoacetophenone 
• 108-24-7 acetic anhydride 

Downstream Products

• 79127-40-5 3-(trifluoroacetamido)-4-nitroacetophenone 
• 1456532-30-1 3-amino-4-nitroacetophenone thiosemicarbazone 
• 79127-39-2 3-(methylamino)-4-nitroacetophenone 
• 92642-29-0 3-(methylamino)-4-aminoacetophenone 
• 92642-17-6 N-(5-acetyl-2-nitrophenyl)acetamide 

Relevant academic research and scientific papers

Green Synthesis of New Pyrrolo [1,2- a ] quinoxalines as Antiproliferative Agents in GPER-expressing Breast Cancer Cells

4,5-Dihydropyrrolo [1,2-a]quinoxalines are interesting druggable scaffolds, with multifaceted biological properties, including anticancer properties targeting the G protein-coupled estrogen receptor 1 (GPER). In this work, the synthesis and preliminary antiproliferative activity of a small set of new 4,5-dihydropyrrolo[1,2-a]quinoxalines (18-20) and pyrrolo[1,2-a]quinoxalines (21, 22) has been reported, inspired by known antiproliferative agents (G-1, G-15, and G-36). The synthesis of the pyrroloquinoxalinic core was employed following the Pictet-Spengler reaction, using the surfactant p-dodecylbenzene sulphonic acid (p-DBSA), as catalyst. It demonstrated efficiency in the catalysis of the 4-phenylpyrrole [1,2-a] quinoxaline type compound formation in mild solvents such as water, ethanol, and hydroalcoholic solutions. In addition, the reactions proceeded in a short time (between 15 and 120 minutes) at room temperature and with high yields. The in vitro MTT assays showed that the presence of isopropyl groups furnished promising antiproliferative compounds. Although, the acetyl group provided also antiproliferative effects, breaking down its responsibility in the GPER transactivation. Nevertheless, it is possible to conclude that the 4,5-dihydropyrrolo[1,2-a]quinoxalines remain a feasible scaffold to develop anticancer agents against GPER-expressing cells.

Design, synthesis and biological evaluation of new aryl thiosemicarbazone as antichagasic candidates

The present work reports on the synthesis, biological assaying and docking studies of a series of 12 aryl thiosemicarbazones, which were planned to act over two main enzymes, cruzain and trypanothione reductase. These enzymes are used as targets of trypanocidal activity in Chagas disease control with a minimal mutagenic profile. Three p-nitroaromatic thiosemicarbazones showed high activity against Trypanosoma cruzi in in vitro assays (IC50 57 μM), and no mutagenic profile was observed in micronucleous tests. Although the in vitro inhibition test showed that 10-μM doses of eight compounds inhibited cruzain activity, no correlation was found between cruzain inhibition and trypanocidal activity.

MEDIATORS OF HEDGEHOG SIGNALING PATHWAYS, COMPOSITIONS AND USES RELATED THERETO

The present invention makes available methods and reagents for inhibiting aberrant growth states resulting from hedgehog gain-of-function, ptc loss-of-function or smoothened gain-of-function comprising contacting the cell with a hedgehog antagonist of formula (I) in a sufficient amount to aberrant growth state, e.g., to agonize a normal ptc pathway or antagonize smoothened or hedgehog activity.

Site-specific labelling of caged ATP with deuterium or 18oxygen

[3-D]2-Nitroacetophenone and [alcohol-18O]-1-(2-nitrophenyl)ethyl alcohol were prepared and used to synthesise labelled P3-1-(2-nitrophenyl)ethyl esters of ATP ('caged ATP') with isotope present either as deuterium on the 3-position of the nitrosubstituted ring or as 18oxygen in the bridging position between the terminal phosphate and the nitrophenylethyl group. The availability of the deuterated compounds enabled complete assignment of their 1H NMR spectra.

Semisynthetic Enzymes: Characterization of Isomeric Flavopapains with Widely Different Catalytic Efficiencies

Flavopapain 6 has been prepared by alkylation of the active site cysteine-25 of papain with 8α-(bromoacetyl)-10-methylisoalloxazine.This semisynthetic enzyme was shown to serve as a catalyst for the oxidation of dihydronicotinamides, exhibiting saturation kinetics and up to 600-fold rate accelerations relative to a model flavin.This is contrasted to the behavior of flavopapain 9, the product of the modification of papain with 6α-(bromoacetyl)-10-methylisoalloxazine.In this case no catalytic rate enhancement compared to the behavior of a model compound is observed.Since the two isoalloxazines are isomeric, the differences in the activities of the semisynthetic enzymes are interpreted in terms of differences in the geometry of the flavin at the active site.It is also noted that flavopapain 6 can exhibit some chiral discrimination toward optically active dihydronicotinamides.