Nosseir, O., Syam, Y., Hashim, A., El-Haggar, R., Anwar, M., Zaghary, W. (2023). In Silico ADME Prediction and Molecular Docking of 1,2,3-Triazole-based Compounds Against Human Aromatase Cytochrome P450. Journal of Advanced Pharmacy Research, 7(4), 232-242. doi: 10.21608/aprh.2023.225722.1231
Ola Nosseir; Yasmin M. Syam; Alaa Hashim; Radwan El-Haggar; Manal M. Anwar; Wafaa Zaghary. "In Silico ADME Prediction and Molecular Docking of 1,2,3-Triazole-based Compounds Against Human Aromatase Cytochrome P450". Journal of Advanced Pharmacy Research, 7, 4, 2023, 232-242. doi: 10.21608/aprh.2023.225722.1231
Nosseir, O., Syam, Y., Hashim, A., El-Haggar, R., Anwar, M., Zaghary, W. (2023). 'In Silico ADME Prediction and Molecular Docking of 1,2,3-Triazole-based Compounds Against Human Aromatase Cytochrome P450', Journal of Advanced Pharmacy Research, 7(4), pp. 232-242. doi: 10.21608/aprh.2023.225722.1231
Nosseir, O., Syam, Y., Hashim, A., El-Haggar, R., Anwar, M., Zaghary, W. In Silico ADME Prediction and Molecular Docking of 1,2,3-Triazole-based Compounds Against Human Aromatase Cytochrome P450. Journal of Advanced Pharmacy Research, 2023; 7(4): 232-242. doi: 10.21608/aprh.2023.225722.1231
In Silico ADME Prediction and Molecular Docking of 1,2,3-Triazole-based Compounds Against Human Aromatase Cytochrome P450
1Department of Pharmaceutical Chemistry, Faculty of Pharmacy, Helwan University, Ain Helwan, Cairo 11795, Egypt
2Department of Therapeutic Chemistry, National Research Center, Dokki, Cairo 12622, Egypt
Abstract
Objective: Inhibition of the human aromatase cytochrome P450 enzyme has been emphasized as being an efficient mechanism for reducing high estrogen levels in the treatment of breast cancer. Methods: Molecular docking and in silico ADME predictions were performed for a set of 1,2,3-triazole-based compounds aiming for the discovery of new therapeutics targeting the human aromatase cytochrome P450 enzyme. Results: The results showed that compounds 1-3 are capable of binding to the enzyme active site, while compounds 4-8 and 9-11 are capable of binding to the potential allosteric sites 1 and 2 of the enzyme, respectively. Furthermore, all compounds 1-7 and 9-11 were predicted to be orally bioavailable, and compounds 1-3, 9, and 11 were anticipated to be blood-brain barrier permeants. Conclusion: Most of the designed compounds possessed relatively good binding affinities to the human placental aromatase cytochrome P450 enzyme and promising in silico ADME-related properties for further optimization towards developing novel human aromatase inhibitors. aromatase inhibitors.
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