1729-01-7Relevant academic research and scientific papers
Spectral switching of naphthalimide-coumarin induced by F-
Li, Xiaochuan,Son, Young-A.
, p. 5370 - 5373 (2015)
A highly selective color sensor based on naphthalimide and coumarin was reported. Upon addition of F-, the solution color changed from pale yellow to deep blue. The sensor shows excellent selectivity against other common anions. The underlying mechanism for the color change is based on the deprotonation/protonation of the dye. Frontier molecular orbitals analysis gives further insight about the signaling mechanism.
Evaluation of novel N′-(3-hydroxybenzoyl)-2-oxo-2H-chromene-3-carbohydrazide derivatives as potential HIV-1 integrase inhibitors
Jesumoroti, Omobolanle J.,Faridoon,Mnkandhla, Dumisani,Isaacs, Michelle,Hoppe, Heinrich C.,Klein, Rosalyn
, p. 80 - 88 (2019/01/30)
In an attempt to identify potential new agents that are active against HIV-1 IN, a series of novel coumarin-3-carbohydrazide derivatives were designed and synthesised. The toxicity profiles of these compounds showed that they were non-toxic to human cells and they exhibited promising anti-HIV-1 IN activities with IC50 values in nM range. Also, an accompanying molecular modeling study showed that the compounds bind to the active pocket of the enzyme.
Design, synthesis and biological evaluation of coumarin derivatives as novel acetylcholinesterase inhibitors that attenuate H2O2-induced apoptosis in SH-SY5Y cells
Yao, Dahong,Wang, Jing,Wang, Guan,Jiang, Yingnan,Shang, Lei,Zhao, Yuqian,Huang, Jian,Yang, Shilin,Wang, Jinhui,Yu, Yamei
, p. 112 - 123 (2016/08/01)
A novel series of coumarin derivatives were designed, synthesized and investigated for inhibition of cholinesterase, including acetyl cholinesterase (AChE) and butyrylcholinesterase (BuChE). This biological study showed that these compounds containing piperazine ring had significant inhibition activities on AChE rather than BuChE. Further study suggested that 9x, as one of this kind of structure derivative, showed the strongest inhibition activity on AChE with an IC50 value of 34?nM. Moreover, molecular docking, flow cytometry (FCM), and western blot assay suggested that 9x could induce cytoprotective autophagy to attenuate H2O2-induced cell death in human neuroblastoma SH-SY5Y cells. These findings highlight a new approach for the development of a novel potential neuroprotective compound targeting AChE with autophagy-inducing activity in future Alzheimer's disease (AD) therapy.
Synthesis and anticholinesterase activity of coumarin-3-carboxamides bearing tryptamine moiety
Ghanei-Nasab, Samaneh,Khoobi, Mehdi,Hadizadeh, Farzin,Marjani, Azam,Moradi, Alireza,Nadri, Hamid,Emami, Saeed,Foroumadi, Alireza,Shafiee, Abbas
, p. 40 - 46 (2016/08/18)
A number of N-(2-(1H-indol-3-yl)ethyl)-2-oxo-2H-chromene-3-carboxamides were synthesized and tested against AChE and BuChE. The in?vitro assessment of the synthesized compounds 4a-o revealed that most of them had significant activity toward AChE. The SAR study demonstrated that the introduction of benzyloxy moiety on the 7-position of coumarin scaffold can improve the anti-AChE activity. The best result was obtained with 7-(4-fluorobenzyl)oxy moiety in the case of compound 4o, displaying IC50value of 0.16?μM. Based on the docking study of AChE, the prototype compound 4o was laid across the active site and occupied both peripheral anionic site (PAS) and catalytic anionic site (CAS).
Novel coumarin-3-carboxamides bearing N-benzylpiperidine moiety as potent acetylcholinesterase inhibitors
Asadipour, Ali,Alipour, Masoumeh,Jafari, Mona,Khoobi, Mehdi,Emami, Saeed,Nadri, Hamid,Sakhteman, Amirhossein,Moradi, Alireza,Sheibani, Vahid,Homayouni Moghadam, Farshad,Shafiee, Abbas,Foroumadi, Alireza
, p. 623 - 630 (2013/12/04)
Abstract Some novel coumarin-3-carboxamide derivatives linked to N-benzylpiperidine scaffold were synthesized and evaluated as acetylcholinesterase (AChE) and butyrylcholinesterase (BuChE) inhibitors. The screening results showed that most of compounds exhibited potent anti-AChE activity in the range of nM concentrations. Among them, compound 10c bearing an N-ethylcarboxamide linker and a 6-nitro substituent showed the most potent activity (IC50 = 0.3 nM) and the highest selectivity (SI = 26,300). Compound 10c was 46-fold more potent than standard drug donepezil against AChE. The kinetic study revealed that compound 10c exhibited mixed-type inhibition against AChE. Protein-ligand docking study demonstrated that the target compounds have dual binding site interaction mode and these results are in agreement with kinetic study.
