57000-49-4

Upstream product

• 3471-31-6 5-methoxy-1H-indole-3-acetic acid 
• 1972-28-7 diethylazodicarboxylate 
• 111795-97-2 ethyl 3-cyano-3-(5-methoxy-2-nitrophenyl)propionate 
• 1006-94-6 5-methoxylindole 
• 105-36-2 ethyl bromoacetate 
• 72963-98-5 ethyl 3-(2-ethoxy-2-oxoethyl)-5-methoxy-1H-indole-2-carboxylate 
• 858232-58-3 3-(carboxymethyl)-5-methoxy-1H-indole-2-carboxylic acid 
• 104-94-9 4-methoxy-aniline 
• 100-17-4 para-methoxynitrobenzene 
• 2436-17-1 5-methoxyindole-3-acetonitrile 
• 64-17-5 ethanol 
• 19501-58-7 4-methoxyphenylhydrazine hydrochloride 
• 2960-66-9 4-oxo-but-2-enoic acid ethyl ester 
• 623-73-4 diazoacetic acid ethyl ester 

Downstream Products

• 712-09-4 5-methoxytryptophol 
• 94685-18-4 5-methoxy-1-(phenylmethyl)-1H-indole-3-acetic acid ethyl ester 
• 221188-38-1 [1-(4-fluoro-phenyl)-5-methoxy-1H-indol-3-yl]-acetic acid ethyl ester 
• 3471-31-6 5-methoxy-1H-indole-3-acetic acid 
• 93879-42-6 1-benzyl-5-methoxy-1H-indole-3-acetamide 
• 93871-13-7 5-methoxy-1-(phenylmethyl)-1H-indole-3-acetic acid hydrazide 
• 164084-32-6 5-methoxy-2-(methylthio)-1-(phenylmethyl)-1H-indole-3-acetamide 
• 57000-48-3 2-(5-methoxy-1H-indol-3-yl)acetohydrazide 
• 1019-45-0 N,N-dimethyl-5-methoxytryptamine 
• 94005-21-7 NSC₅₄₇₇₁ 

Relevant academic research and scientific papers

Fe-catalyzed Fukuyama-type indole synthesis triggered by hydrogen atom transfer

Fe, Co, and Mn hydride-initiated radical olefin additions have enjoyed great success in modern synthesis, yet the extension of other hydrogen radicalophiles instead of olefins remains largely elusive. Herein, we report an efficient Fe-catalyzed intramolec

INDOLEACETIC ACID DERIVATIVE AND PREPARATION METHOD AND PHARMACEUTICAL USE THEREOF

The present invention relates to an indoleacetic acid derivative and a preparation method and pharmaceutical use thereof. In particular, the present invention relates to a compound shown in general formula (I), a preparation method thereof, a pharmaceutical composition comprising the same, and a use thereof as a cough suppressant in treating a disease such as a cough. The definition of each substituent in the general formula (I) is the same as the definition in the specification.

Directed Evolution of a Cytochrome P450 Carbene Transferase for Selective Functionalization of Cyclic Compounds

Transfers of carbene moieties to heterocycles or cyclic alkenes to obtain C(sp2)-H alkylation or cyclopropane products are valuable transformations for synthesis of pharmacophores and chemical building blocks. Through their readily tunable active-site geometries, hemoprotein "carbene transferases" could provide an alternative to traditional transition metal catalysts by enabling heterocycle functionalizations with high chemo-, regio-, and stereocontrol. However, carbene transferases accepting heterocyclic substrates are scarce; the few enzymes capable of heterocycle or cyclic internal alkene functionalization described to date are characterized by low turnovers or depend on artificially introduced, costly iridium-porphyrin cofactors. We addressed this challenge by evolving a cytochrome P450 for highly efficient carbene transfer to indoles, pyrroles, and cyclic alkenes. We first developed a spectrophotometric high-throughput screening assay based on 1-methylindole C3-alkylation that enabled rapid analysis of thousands of P450 variants and comprehensive directed evolution via random and targeted mutagenesis. This effort yielded a P450 variant with 11 amino acid substitutions and a large deletion of the non-catalytic P450 reductase domain, which chemoselectively C3-alkylates indoles with up to 470 turnovers per minute and 18000 total turnovers. We subsequently used this optimized alkylation variant for parallel evolution toward more challenging heterocycle carbene functionalizations, including C2/C3 regioselective pyrrole alkylation, enantioselective indole alkylation with ethyl 2-diazopropanoate, and cyclic internal alkene cyclopropanation. The resulting set of efficient biocatalysts showcases the tunability of hemoproteins for highly selective functionalization of cyclic targets and the power of directed evolution to enhance the scope of new-to-nature enzyme catalysts.

Myoglobin-Catalyzed C?H Functionalization of Unprotected Indoles

Functionalized indoles are recurrent motifs in bioactive natural products and pharmaceuticals. While transition metal-catalyzed carbene transfer has provided an attractive route to afford C3-functionalized indoles, these protocols are viable only in the presence of N-protected indoles, owing to competition from the more facile N?H insertion reaction. Herein, a biocatalytic strategy for enabling the direct C?H functionalization of unprotected indoles is reported. Engineered variants of myoglobin provide efficient biocatalysts for this reaction, which has no precedents in the biological world, enabling the transformation of a broad range of indoles in the presence of ethyl α-diazoacetate to give the corresponding C3-functionalized derivatives in high conversion yields and excellent chemoselectivity. This strategy could be exploited to develop a concise chemoenzymatic route to afford the nonsteroidal anti-inflammatory drug indomethacin.

A Cooperative Hydrogen Bond Donor–Br?nsted Acid System for the Enantioselective Synthesis of Tetrahydropyrans

Carbocations stabilized by adjacent oxygen atoms are useful reactive intermediates involved in fundamental chemical transformations. These oxocarbenium ions typically lack sufficient electron density to engage established chiral Br?nsted or Lewis acid catalysts, presenting a major challenge to their widespread application in asymmetric catalysis. Leading methods for selectivity operate primarily through electrostatic pairing between the oxocarbenium ion and a chiral counterion. A general approach to new enantioselective transformations of oxocarbenium ions requires novel strategies that address the weak binding capabilities of these intermediates. We demonstrate herein a novel cooperative catalysis system for selective reactions with oxocarbenium ions. This new strategy has been applied to a highly selective and rapid oxa-Pictet–Spengler reaction and highlights a powerful combination of an achiral hydrogen bond donor with a chiral Br?nsted acid.

Tert-Butyl Iodide Mediated Reductive Fischer Indolization of Conjugated Hydrazones

A novel reductive Fischer indolization of readily available N-aryl conjugated hydrazones with tert-butyl iodide has been developed. In this reaction, tert-butyl iodide is used as anhydrous HI source, and the generated HI acts as a Br?nsted acid and a reducing agent. This operationally simple method allows access to various indole derivatives. Furthermore, the procedure can be applied to the synthesis of biologically active compounds.

Novel N -Acetyl Bioisosteres of Melatonin: Melatonergic Receptor Pharmacology, Physicochemical Studies, and Phenotypic Assessment of Their Neurogenic Potential

Herein we present a new family of melatonin-based compounds, in which the acetamido group of melatonin has been bioisosterically replaced by a series of reversed amides and azoles, such as oxazole, 1,2,4-oxadiazole, and 1,3,4-oxadiazole, as well as other related five-membered heterocycles, namely, 1,3,4-oxadiazol(thio)ones, 1,3,4-triazol(thio)ones, and an 1,3,4-thiadiazole. New compounds were fully characterized at melatonin receptors (MT1R and MT2R), and results were rationalized by superimposition studies of their structures to the bioactive conformation of melatonin. We also found that several of these melatonin-based compounds promoted differentiation of rat neural stem cells to a neuronal phenotype in vitro, in some cases to a higher extent than melatonin. This unique profile constitutes the starting point for further pharmacological studies to assess the mechanistic pathways and the relevance of neurogenesis induced by melatonin-related structures.

Discovery and refinement of a new structural class of potent peptide deformylase inhibitors

New classes of antibiotics are urgently needed to counter increasing levels of pathogen resistance. Peptide deformylase (PDF) was originally selected as a specific bacterial target, but a human homologue, the inhibition of which causes cell death, was rec

New N-(pyridin-4-yl)-(indol-3-yl)acetamides and propanamides as antiallergic agents

A series of new N-(pyridin-4-yl)-(indol-3-yl)alkylamides 44-84 has been prepared in the search of novel antiallergic compounds. Synthesis of the desired ethyl (2-methyindol-3-yl)acetates 1-4 was achieved by indolization under Fischer conditions; Japp-Klingemann method followed by 2- decarboxylation afforded the ethyl (indol-3-yl)alkanoates 17-25. Amidification was successfully carried out by condensation of the corresponding acids or their N-aryl(methyl) derivatives with 4-aminopyridine promoted by 2-chloro-1-methylpyridinium iodide. Efforts to improve the antiallergic potency of the title series by variation of the indole substituents (R1, R2, R) and the length of the alkanoic chain (n = 1, 2, 3) led to the selection of N-(pyridin-4-yl)-[1-(4-fluorobenzyl)indol-3- yl]acetamide 45, out of 41 compounds. This amide was 406-fold more potent than astemizole in the ovalbumin-induced histamine release assay, using guinea pig peritoneal mast cells, with an IC50 = 0.016 μM. Its inhibitory activity in IL-4 production test from Th-2 cells was identical to that of the reference histamine antagonist (IC50 = 8.0 μM) and twice higher in IL-5 assay: IC50 = 1.5 and 3.3 μM, respectively. In vivo antiallergic activity evaluation confirmed efficiency of 45 in sensitized guinea pig late phase eosinophilia inhibition, after parenteral and oral administration at 5 and 30 mg/kg, respectively. Its efficiency in inhibition of microvascular permeability was assessed in two rhinitis models; ovalbumin and capsaicin- induced rhinorrhea could be prevented after topical application of submicromolar concentrations of 45 (IC50 = 0.25 and 0.30 μM); and it also exerted significant inhibitory effect in the first test after iv and oral administration, with ID50 = 0.005 and 0.46 mg/kg.

1H-INDOLE-3-ACETAMIDE SPLA2 INHIBITORS

A class of novel 1-indole-3-acetamides represented by the formula; is disclosed together with the use of such indole compounds for inhibiting sPLA2 mediated release of fatty acids.