Discovery of mixed type thymidine phosphorylase inhibitors endowed with antiangiogenic properties: Synthesis, pharmacological evaluation and molecular docking study of 2-thioxo-pyrazolo[1,5-a][1,3,5]triazin-4-ones. Part II

2014 ◽  
Vol 78 ◽  
pp. 294-303 ◽  
Author(s):  
Hriday Bera ◽  
Probir kumar Ojha ◽  
Bee Jen Tan ◽  
Lingyi Sun ◽  
Anton V. Dolzhenko ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Thymidine Phosphorylase ◽  
Mixed Type ◽  
Docking Study ◽  
Molecular Docking Study ◽  
Pharmacological Evaluation

Synthesis, thymidine phosphorylase, angiogenic inhibition and molecular docking study of isoquinoline derivatives

2019 ◽  
Vol 89 ◽  
pp. 102999 ◽  
Author(s):  
Khalid Zaman ◽  
Fazal Rahim ◽  
Muhammad Taha ◽  
Abdul Wadood ◽  
Syed Adnan Ali Shah ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Thymidine Phosphorylase ◽  
Docking Study ◽  
Molecular Docking Study ◽  
Isoquinoline Derivatives

scholarly journals Synthesis of Thymidine Phosphorylase Inhibitor Based on Quinoxaline Derivatives and Their Molecular Docking Study

Molecules ◽  
2019 ◽  
Vol 24 (6) ◽  
pp. 1002 ◽  
Author(s):  
Noor Almandil ◽  
Muhammad Taha ◽  
Rai Farooq ◽  
Amani Alhibshi ◽  
Mohamed Ibrahim ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Thymidine Phosphorylase ◽  
Docking Study ◽  
Docking Studies ◽  
Molecular Docking Study ◽  
Substitution Pattern ◽  
Structure Activity ◽  
Ic50 Value ◽  
Quinoxaline Derivatives ◽  
Better Than

We have synthesized quinoxaline analogs (1–25), characterized by 1H-NMR and HREI-MS and evaluated for thymidine phosphorylase inhibition. Among the series, nineteen analogs showed better inhibition when compared with the standard inhibitor 7-Deazaxanthine (IC50 = 38.68 ± 4.42 µM). The most potent compound among the series is analog 25 with IC50 value 3.20 ± 0.10 µM. Sixteen analogs 1, 2, 3, 4, 5, 6, 7, 12, 13, 14, 15, 16, 17, 18, 21 and 24 showed outstanding inhibition which is many folds better than the standard 7-Deazaxanthine. Two analogs 8 and 9 showed moderate inhibition. A structure-activity relationship has been established mainly based upon the substitution pattern on the phenyl ring. The binding interactions of the active compounds were confirmed through molecular docking studies.

Synthesis, molecular docking study and thymidine phosphorylase inhibitory activity of 3-formylcoumarin derivatives

2018 ◽  
Vol 78 ◽  
pp. 17-23 ◽  
Author(s):  
Muhammad Taha ◽  
Syed Adnan Ali Shah ◽  
Muhammad Afifi ◽  
Syahrul Imran ◽  
Sadia Sultan ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Inhibitory Activity ◽  
Thymidine Phosphorylase ◽  
Docking Study ◽  
Molecular Docking Study

Synthesis, SAR elucidations and molecular docking study of newly designed isatin based oxadiazole analogs as potent inhibitors of thymidine phosphorylase

2018 ◽  
Vol 79 ◽  
pp. 323-333 ◽  
Author(s):  
Muhammad Tariq Javid ◽  
Fazal Rahim ◽  
Muhammad Taha ◽  
Mohsan Nawaz ◽  
Abdul Wadood ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Thymidine Phosphorylase ◽  
Docking Study ◽  
Molecular Docking Study

Computational and Kinetic Studies of Acetylcholine Esterase Inhibition by Phenserine

2019 ◽  
Vol 25 (18) ◽  
pp. 2108-2112 ◽  
Author(s):  
Shams Tabrez ◽  
Ghazi A. Damanhouri
Keyword(s):  
Molecular Docking ◽  
Mixed Type ◽  
Kinetic Studies ◽  
Docking Study ◽  
Docking Studies ◽  
Catalytic Site ◽  
Dependent Manner ◽  
Molecular Docking Study ◽  
Ic50 Value ◽  
Current Article

Background: The inhibition of cholinesterase enzymes is one of the promising strategies to manage several neurological disorders that include Alzheimer's disease (AD). Material and Methods: In the current article, we estimated the potential inhibition of acetyl cholinesterase (AChE) by phenserine using slightly modified Ellman assay. To find out the binding interactions of phenserine with the catalytic site of AChE, a molecular docking study was also performed. Results: Phenserine was found to inhibit Electrophorus electricus AChE in a dose-dependent manner with an IC50 value of 0.013 µM. The kinetic analyses indicate that phenserine inhibits AChE in a mixed type manner (competitive and uncompetitive) with Ki values of 0.39 μmole/l and 0.21 µmole/l, respectively. On the other hand, Km and Vmax values were found to be 0.17 µM and 0.39 µM, respectively. The molecular docking studies indicate efficient binding of phenserine through 6 hydrogen bonds, 4 pi-alkyl interactions, and 1 pi-pi interaction within the AChE catalytic pocket. Conclusion: Results of our computational and kinetics studies indicated a mixed type inhibition by phenserine at AChE catalytic site.

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