MIND-BEST: Web Server for Drugs and Target Discovery; Design, Synthesis, and Assay of MAO-B Inhibitors and Theoretical−Experimental Study of G3PDH Protein fromTrichomonas gallinae

2011 ◽  
Vol 10 (4) ◽  
pp. 1698-1718 ◽  
Author(s):  
Humberto González-Díaz ◽  
Francisco Prado-Prado ◽  
Xerardo García-Mera ◽  
Nerea Alonso ◽  
Paula Abeijón ◽  
...  
Keyword(s):  
Experimental Study ◽  
Web Server ◽  
Design Synthesis ◽  
Target Discovery ◽  
Mao B

scholarly journals Design, synthesis, molecular modelling and in vitro screening of monoamine oxidase inhibitory activities of novel quinazolyl hydrazine derivatives

2020 ◽  
Vol 7 (4) ◽  
pp. 200050
Author(s):  
Adel Amer ◽  
Abdelrahman H. Hegazi ◽  
Mohammed Khalil Alshekh ◽  
Hany E. A. Ahmed ◽  
Saied M. Soliman ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Monoamine Oxidase ◽  
In Vitro Screening ◽  
Phenyl Substituent ◽  
Design Synthesis ◽  
Mao B ◽  
Mao A ◽  
Ft Ir ◽  
Inhibitory Activities

A new series of N'-substituted benzylidene-2-(4-oxo-2-phenyl-1,4-dihydroquinazolin-3(2H)-yl)acetohydrazide ( 5a–5h ) has been synthesized, characterized by FT-IR, NMR spectroscopy and mass spectrometry and tested against human monoamine oxidase (MAO) A and B. Only (4-hydroxy-3-methoxybenzylidene) substituted compounds gave submicromolar inhibition of MAO-A and MAO-B. Changing the phenyl substituent to methyl on the unsaturated quinazoline ring ( 12a–12d ) decreased inhibition, but a less flexible linker ( 14a–14d ) resulted in selective micromolar inhibition of hMAO-B providing insight for ongoing design.

scholarly journals Pyrazolobenzothiazine-based carbothioamides as new structural leads for the inhibition of monoamine oxidases: design, synthesis, in vitro bioevaluation and molecular docking studies

MedChemComm ◽  
2017 ◽  
Vol 8 (2) ◽  
pp. 452-464 ◽  
Author(s):  
Syed Mobasher Ali Abid ◽  
Sana Aslam ◽  
Sumera Zaib ◽  
Syeda Mahwish Bakht ◽  
Matloob Ahmad ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Active Site ◽  
Potent Inhibitor ◽  
Binding Mode ◽  
Docking Studies ◽  
Design Synthesis ◽  
Molecular Docking Studies ◽  
Monoamine Oxidases ◽  
Mao B

Binding mode of potent inhibitor (green) & cognate ligand (pink) in the active site of MAO-B.

scholarly journals NL MIND-BEST: A web server for ligands and proteins discovery—Theoretic-experimental study of proteins of Giardia lamblia and new compounds active against Plasmodium falciparum

2011 ◽  
Vol 276 (1) ◽  
pp. 229-249 ◽  
Author(s):  
Humberto González-Díaz ◽  
Francisco Prado-Prado ◽  
Eduardo Sobarzo-Sánchez ◽  
Mohamed Haddad ◽  
Séverine Maurel Chevalley ◽  
...  
Keyword(s):  
Experimental Study ◽  
Plasmodium Falciparum ◽  
Giardia Lamblia ◽  
Web Server ◽  
New Compounds

scholarly journals Design, Synthesis, and Biological Evaluation of Pyridazinones Containing the (2-Fluorophenyl) Piperazine Moiety as Selective MAO-B Inhibitors

Molecules ◽  
2020 ◽  
Vol 25 (22) ◽  
pp. 5371
Author(s):  
Muhammed Çeçen ◽  
Jong Min Oh ◽  
Zeynep Özdemir ◽  
Saliha Ebru Büyüktuncel ◽  
Mehtap Uysal ◽  
...  
Keyword(s):  
Biological Evaluation ◽  
Inhibitory Potency ◽  
Design Synthesis ◽  
Docking Simulations ◽  
Mao B ◽  
Ic50 Value ◽  
Competitive Inhibitors ◽  
Mao A ◽  
Ic50 Values ◽  
Synthesis And Biological Evaluation

Twelve pyridazinones (T1–T12) containing the (2-fluorophenyl) piperazine moiety were designed, synthesized, and evaluated for monoamine oxidase (MAO) -A and -B inhibitory activities. T6 was found to be the most potent MAO-B inhibitor with an IC50 value of 0.013 µM, followed by T3 (IC50 = 0.039 µM). Inhibitory potency for MAO-B was more enhanced by meta bromo substitution (T6) than by para bromo substitution (T7). For para substitution, inhibitory potencies for MAO-B were as follows: -Cl (T3) > -N(CH3)2 (T12) > -OCH3 (T9) > Br (T7) > F (T5) > -CH3 (T11) > -H (T1). T6 and T3 efficiently inhibited MAO-A with IC50 values of 1.57 and 4.19 µM and had the highest selectivity indices (SIs) for MAO-B (120.8 and 107.4, respectively). T3 and T6 were found to be reversible and competitive inhibitors of MAO-B with Ki values of 0.014 and 0.0071, respectively. Moreover, T6 was less toxic to healthy fibroblast cells (L929) than T3. Molecular docking simulations with MAO binding sites returned higher docking scores for T6 and T3 with MAO-B than with MAO-A. These results suggest that T3 and T6 are selective, reversible, and competitive inhibitors of MAO-B and should be considered lead candidates for the treatment of neurodegenerative disorders like Alzheimer’s disease.

Design, synthesis and biological evaluation of oxygenated chalcones as potent and selective MAO-B inhibitors

2019 ◽  
Vol 93 ◽  
pp. 103335 ◽  
Author(s):  
Della Grace Thomas Parambi ◽  
Jong Min Oh ◽  
Seung Cheol Baek ◽  
Jae Pil Lee ◽  
Anna Rita Tondo ◽  
...  
Keyword(s):  
Biological Evaluation ◽  
Design Synthesis ◽  
Mao B ◽  
Synthesis And Biological Evaluation

Target discovery of chlorogenic acid derivatives from the flower buds of Lonicera macranthoides and their MAO B inhibitory mechanism

Fitoterapia ◽  
2019 ◽  
Vol 134 ◽  
pp. 297-304 ◽  
Author(s):  
Yudan Mei ◽  
Dabo Pan ◽  
Yingnan Jiang ◽  
Weiyang Zhang ◽  
Xiaojun Yao ◽  
...  
Keyword(s):  
Chlorogenic Acid ◽  
Inhibitory Mechanism ◽  
Flower Buds ◽  
Target Discovery ◽  
Mao B ◽  
Lonicera Macranthoides

Design, Synthesis, in vitro MAO-B Inhibitory Evaluation, and Computational Studies of Some 6-Nitrobenzothiazole-Derived Semicarbazones

ChemMedChem ◽  
2013 ◽  
Vol 8 (3) ◽  
pp. 462-474 ◽  
Author(s):  
Rati K. P. Tripathi ◽  
Omprakash Goshain ◽  
Senthil Raja Ayyannan
Keyword(s):  
Computational Studies ◽  
Design Synthesis ◽  
Mao B
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