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AKOS B014994 is a chemical compound derived from phenethylamine and classified under the benzylamine class. It serves as an intermediate in organic synthesis and drug development, with potential implications in the inhibition of monoamine oxidase, an enzyme crucial for neurotransmitter metabolism, including dopamine and serotonin. This characteristic hints at its possible therapeutic applications in treating conditions like depression and anxiety, although further research is necessary to elucidate its full pharmacological profile and potential uses.
Usage:
Used in Pharmaceutical Industry:
AKOS B014994 is used as a chemical intermediate for the synthesis of various pharmaceutical compounds, leveraging its structural properties to facilitate the development of new drugs.
Used in Neurotransmitter Research:
AKOS B014994 is used as a research tool to study the role of monoamine oxidase in the metabolism of neurotransmitters like dopamine and serotonin, which is instrumental in understanding the mechanisms of mood disorders.
Used in Drug Development for Mood Disorders:
AKOS B014994 is considered for potential therapeutic applications in the treatment of mood disorders such as depression and anxiety due to its implication in inhibiting monoamine oxidase, a key enzyme in neurotransmitter metabolism.
Used in Organic Synthesis:
AKOS B014994 is utilized as a building block in organic synthesis to create a variety of chemical compounds for different applications, including but not limited to pharmaceuticals, agrochemicals, and materials science.

7732-44-7

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7732-44-7 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 7732-44-7 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 7,7,3 and 2 respectively; the second part has 2 digits, 4 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 7732-44:
(6*7)+(5*7)+(4*3)+(3*2)+(2*4)+(1*4)=107
107 % 10 = 7
So 7732-44-7 is a valid CAS Registry Number.
InChI:InChI=1/C11H10N2O2/c12-13-11(15)9-6-5-7-3-1-2-4-8(7)10(9)14/h1-6,14H,12H2,(H,13,15)

7732-44-7SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 19, 2017

Revision Date: Aug 19, 2017

1.Identification

1.1 GHS Product identifier

Product name 1-hydroxynaphthalene-2-carbohydrazide

1.2 Other means of identification

Product number -
Other names 2-???naphthol

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:7732-44-7 SDS

7732-44-7Relevant academic research and scientific papers

Synthesis and Anti-Proliferative Activity of Sulfanyltriazolylnaphthalenols and Sulfanyltriazolylnaphthalene-1,4-diones

Chaaban, Ibrahim,El Khawass, El Sayeda M.,Abd El Razik, Heba A.,El Salamouni, Nehad S.,Redondo-Horcajo, Mariano,Barasoain, Isabel,Díaz, José Fernando,Yli-Kauhaluoma, Jari,Moreira, Vania M.

, p. 749 - 761 (2016)

A series of new sulfanyltriazolylnaphthalenols (10a–f and 13a–f) and sulfanyltriazolylnaphthalene-1,4-diones (14a–f) were synthesized and evaluated against a panel of cancer cell lines. Among the tested compounds, 10b and 10d showed the best anti-prolifer

Inhibitory potential of new phenolic hydrazide-hydrazones with a decoy substrate fragment towards laccase from a phytopathogenic fungus: SAR and molecular docking studies

Giurg, Miros?aw,Maniak, Halina,Talma, Micha?

, (2021/11/17)

Laccase from pathogenic fungi participates in both the delignification and neutralization of phytoantibiotics. Furthermore, it interferes with the hormone signaling in plants and catalyzes melanization. Infections of these pathogens contribute to loss in

4-Amino-1,2,4-triazole-3-thione-derived Schiff bases as metallo-β-lactamase inhibitors

Baud, Damien,Bebrone, Carine,Becker, Katja,Benvenuti, Manuela,Cerboni, Giulia,Chelini, Giulia,Cutolo, Giuliano,De Luca, Filomena,Docquier, Jean-Denis,Feller, Georges,Fischer, Marina,Galleni, Moreno,Gavara, Laurent,Gresh, Nohad,Kwapien, Karolina,Legru, Alice,Mangani, Stefano,Mercuri, Paola,Pozzi, Cecilia,Sannio, Filomena,Sevaille, Laurent,Tanfoni, Silvia,Verdirosa, Federica,Berthomieu, Dorothée,Bestgen, Beno?t,Frère, Jean-Marie,Hernandez, Jean-Fran?ois

supporting information, (2020/09/16)

Resistance to β-lactam antibiotics in Gram-negatives producing metallo-β-lactamases (MBLs) represents a major medical threat and there is an extremely urgent need to develop clinically useful inhibitors. We previously reported the original binding mode of 5-substituted-4-amino/H-1,2,4-triazole-3-thione compounds in the catalytic site of an MBL. Moreover, we showed that, although moderately potent, they represented a promising basis for the development of broad-spectrum MBL inhibitors. Here, we synthesized and characterized a large number of 4-amino-1,2,4-triazole-3-thione-derived Schiff bases. Compared to the previous series, the presence of an aryl moiety at position 4 afforded an average 10-fold increase in potency. Among 90 synthetic compounds, more than half inhibited at least one of the six tested MBLs (L1, VIM-4, VIM-2, NDM-1, IMP-1, CphA) with Ki values in the μM to sub-μM range. Several were broad-spectrum inhibitors, also inhibiting the most clinically relevant VIM-2 and NDM-1. Active compounds generally contained halogenated, bicyclic aryl or phenolic moieties at position 5, and one substituent among o-benzoic, 2,4-dihydroxyphenyl, p-benzyloxyphenyl or 3-(m-benzoyl)-phenyl at position 4. The crystallographic structure of VIM-2 in complex with an inhibitor showed the expected binding between the triazole-thione moiety and the dinuclear centre and also revealed a network of interactions involving Phe61, Tyr67, Trp87 and the conserved Asn233. Microbiological analysis suggested that the potentiation activity of the compounds was limited by poor outer membrane penetration or efflux. This was supported by the ability of one compound to restore the susceptibility of an NDM-1-producing E. coli clinical strain toward several β-lactams in the presence only of a sub-inhibitory concentration of colistin, a permeabilizing agent. Finally, some compounds were tested against the structurally similar di-zinc human glyoxalase II and found weaker inhibitors of the latter enzyme, thus showing a promising selectivity towards MBLs.

Discovering potent inhibitors against the β-hydroxyacyl-acyl carrier protein dehydratase (FabZ) of helicobacter pylori: Structure-based design, synthesis, bioassay, and crystal structure determination

He, Lingyan,Zhang, Liang,Liu, Xiaofeng,Li, Xianghua,Zheng, Mingyue,Li, HongLin,Yu, Kunqian,Chen, Kaixian,Shen, Xu,Jiang, Hualiang,Liu, Hong

experimental part, p. 2465 - 2481 (2010/03/03)

The discovery of HpFabZ inhibitors is now of special interest in the treatment of various gastric diseases. In this work, three series of derivatives (compounds 3, 4, and 5) were designed, synthesized, and their biological activities were investigated as potential HpFabZ inhibitors in a two phased manner. First, we designed and synthesized two series of derivatives (3a-r and 4a-u) and evaluated the enzyme-based assay against HpFabZ. Five compounds (3i-k, 3m, and 3q) showed potential inhibitory activity, with IC50 values less than 2 μM. Second, a focused combinatorial library containing 280 molecules was designed employing the LD1.0 program. Twelve compounds (5a-l) were selected and synthesized. The activity of the most potent compound 5h (IC 50) 0.86 μM) was 46 times higher than that of the hit 1. The high hit rate and the potency of the new HpFabZ inhibitors demonstrated the efficiency of the strategy for the focused library design and virtual screening.

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