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2-amino-N-(4-methoxyphenyl)propanamide is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

220903-53-7

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220903-53-7 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 220903-53-7 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 2,2,0,9,0 and 3 respectively; the second part has 2 digits, 5 and 3 respectively.
Calculate Digit Verification of CAS Registry Number 220903-53:
(8*2)+(7*2)+(6*0)+(5*9)+(4*0)+(3*3)+(2*5)+(1*3)=97
97 % 10 = 7
So 220903-53-7 is a valid CAS Registry Number.

220903-53-7Relevant academic research and scientific papers

New sulphonamide pyrolidine carboxamide derivatives: Synthesis, molecular docking, antiplasmodial and antioxidant activities

Onoabedje, Efeturi A.,Ibezim, Akachukwu,Okoro, Uchechukwu C.,Batra, Sanjay

, (2021/03/16)

Carboxamides bearing sulphonamide functionality have been shown to exhibit significant lethal effect on Plasmodium falciparum, the causative agent of human malaria. Here we report the synthesis of thirty-two new drug-like sulphonamide pyrolidine carboxami

Structure-based discovery of highly selective phosphodiesterase-9A inhibitors and implications for inhibitor design

Meng, Fei,Huang, Manna,Zhu, Xinhai,Wan, Yiqian,Hou, Jing,Shao, Yong-Xian,Cai, Yonghong,Li, Zhe,Xu, Jie,Liu, Peiqing,Luo, Hai-Bin,Ke, Hengming,Wu, Pei-Ying

, p. 8549 - 8558,10 (2020/09/15)

A new series of phosphodiesterase-9 (PDE9) inhibitors that contain a scaffold of 6-amino-pyrazolopyrimidinone have been discovered by a combination of structure-based design and computational docking. This procedure significantly saved the load of chemical synthesis and is an effective method for the discovery of inhibitors. The best compound 28 has an IC50 of 21 nM and 3.3 μM, respectively, for PDE9 and PDE5 and about 3 orders of magnitude of selectivity against other PDE families. The crystal structure of the PDE9 catalytic domain in complex with 28 has been determined and shows a hydrogen bond between 28 and Tyr424. This hydrogen bond may account for the 860-fold selectivity of 28 against PDE1B, in comparison with about 30-fold selectivity of BAY73-6691. Thus, our studies suggest that Tyr424, a unique residue of PDE8 and PDE9, is a potential target for improvement of selectivity of PDE9 inhibitors.

N-substituted 2-(2,6-dinitrophenylamino)propanamides: Novel prodrugs that release a primary amine via nitroreduction and intramolecular cyclization

Sykes, Bridget M.,Atwell, Graham J.,Hogg, Alison,Wilson, William R.,O'Connor, Charmian J.,Denny, William A.

, p. 346 - 355 (2007/10/03)

A series of N-dinitrophenylamino acid amides [(4-CONHZ-2,6- diNO'2Ph)N(R)C(X,Y)CONHPhOMe] were prepared as potential bioreductive prodrugs and reduced radiolytically to study their rates of subsequent intramolecular cyclization. Compounds bearing a free NH group (R = H) underwent rapid cyclization in neutral aqueous buffers (t(1/2) 1 min) following 4-electron reduction, with the generation of a N- hydroxydihydroquinoxalinone and concomitant release of 4-methoxyaniline. Amine release from analogous N-methyl analogues (R = Me) was relatively slow. These results are consistent with intramolecular cyclization of a monohydroxylamine intermediate. The high rates of cyclization/extrusion by these very electron-deficient hydroxylamines suggest that the process is greatly accelerated by the presence of an H-bonding 'conformational lock' between the anilino NH group and the adjacent o-nitro group (Kirk and Cohen, 1972). Changes in the phenylcarboxamide side chain or in C-methylation in the linking chain had little effect on the rate of cyclization. The model compounds had 1-electron reduction potentials in the range appropriate for cellular reduction (-373 mV for a measured example) and appeared suitable for development as prodrugs that release amine-based effectors following enzymic or radiolytic reduction. Prodrug examples containing 4-aminoaniline mustard and 5-amino-1-(chloromethyl)benz[e]indoline alkylating units were evaluated but were not activated efficiently by cellular nitroreductases. However, cell killing by the radiation-induced reduction of the latter prodrug was demonstrated.

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