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Research Article

Synthesis and Molecular Docking Study of bis-thiobarbiturate Derivatives as Effective Inhibitors of beta-glucuronidase

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Dr. Hayat Ullah , Fahad Khan , Fazal Rahim , Zia Ur Rehman , Muhammad Taha , Abdul Wadood , Fawad Ahmad , Zainul Wahab , Imad Uddin , Khalid Zaman , Name not found
J Ong Chem Res, 2019, 4 (1), 32-36, DOI: https://doi.org/10.5281/zenodo.3576583, ISSN 2651-4338
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Abstract

Bis-thiobarbiturate derivatives 1-15 have been synthesized and evaluated for their in vitro β-glucuronidase inhibitory potential. The structures of all compounds were confirmed through spectroscopic techniques such as EI-MS and 1HNMR. Compounds 13 (IC50 = 29.42 ± 0.61µM) showed potent β-glucuronidase inhibitory potential better than the standard inhibitor (D-saccharic acid 1, 4 lactone, IC50 = 48.4 ± 1.25 µM). The compounds 2 (IC50 = 48.45 ± 0.39 µM), 3 (IC50 = 53.12 ± 0.22 µM), 4 (IC50 = 55.12 ± 1.13µM) and 9 (IC50 = 49.84 ±1.46µM) showed b-glucuronidase inhibitory potential comparable to the standard inhibitor. Compounds 1 (IC50 = 68.45 ± 0.33 µM), 5 (IC50 = 61.18 ± 1.42µM), 6 (IC50 = 92.57 ±2.80 µM), 7 (IC50 = 61.27 ± 0.45 µM), 8 (IC50 = 62.85 ± 0.79µM), and 12 (IC50 = 77.56 ± 1.32µM) also showed good inhibitory potential. The remaining compounds are found to be completely inactive. The structure-activity relationship was established for these compounds. This study identified a novel class of β-glucuronidase inhibitors.

Keywords organic synthesis Molecular docking studies Thiobarbituric acid β-glucuronidase Inhibition thiobarbiturate
Authors 11
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The team behind this paper

11 authors, 6 institutions.

This paper University of Okara — Pakistan University of Okara 1 author Hazara University Mansehra — Pakistan Hazara University Manse… 5 authors University of Dammam — Saudi Arabia University of Dammam 1 author Abdul Wali Khan University Mardan — Pakistan Abdul Wali Khan Univers… 1 author Hazara University — Pakistan Hazara University 2 authors appreview@scimatic.org appreview@scimatic.org 1 author Dr. Hayat Ullah HU Dr. Hayat Ullah Fahad Khan FK Fahad Khan Fazal Rahim FR Fazal Rahim Zia Ur Rehman ZR Zia Ur Rehman Imad Uddin — corresponding author IU Imad Uddin ✉ Khalid Zaman KZ Khalid Zaman Muhammad Taha MT Muhammad Taha Abdul Wadood AW Abdul Wadood Fawad Ahmad FA Fawad Ahmad Zainul Wahab ZW Zainul Wahab Unknown author UA Unknown author

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SciMatic 0xc35709…277732 100,000 (10%)
Dr. Hayat Ullah 0x15737B…664aCA 90,000 (9%)
Fahad Khan 0x2A6135…1C1882 90,000 (9%)
Fazal Rahim 0x53De81…e8Ba4C 90,000 (9%)
Zia Ur Rehman 0xD5a169…55F925 90,000 (9%)
Muhammad Taha 0x2F922e…e35Baf 90,000 (9%)
Abdul Wadood 0xB3cE3B…eA394A 90,000 (9%)
Fawad Ahmad 0x714e75…9e6Bfb 90,000 (9%)
Zainul Wahab 0xd23C46…11FD62 90,000 (9%)
Imad Uddin 0x455B3e…4cE434 90,000 (9%)
Khalid Zaman 0xB1e0e3…5B5800 90,000 (9%)
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Bibliographic Information

Dr. Hayat Ullah, Fahad Khan, Fazal Rahim, Zia Ur Rehman, Muhammad Taha, Abdul Wadood, Fawad Ahmad, Zainul Wahab, Imad Uddin, Khalid Zaman, name not found (2019). Synthesis and Molecular Docking Study of bis-thiobarbiturate Derivatives as Effective Inhibitors of beta-glucuronidase, Journal of Ongoing Chemical Research, 4(1): 32-36
Bibtex Citation
@article{imad_uddin2019jocr,
author = {Dr. Hayat Ullah and Fahad Khan and Fazal Rahim and Zia Ur Rehman and Muhammad Taha and Abdul Wadood and Fawad Ahmad and Zainul Wahab and Imad Uddin and Khalid Zaman and name not found},
title = {Synthesis and Molecular Docking Study of bis-thiobarbiturate Derivatives as Effective Inhibitors of beta-glucuronidase},
journal = {Journal of Ongoing Chemical Research},
year = {2019},
volume = {4},
number = {1},
pages = {32-36},
doi = {10.5281/zenodo.3576583},
url = {https://scimatic.org/show_manuscript/163}
}
APA Citation
Ullah, D.H., Khan, F., Rahim, F., Rehman, Z.U., Taha, M., Wadood, A., Ahmad, F., Wahab, Z., Uddin, I., Zaman, K., found, n.n., (2019). Synthesis and Molecular Docking Study of bis-thiobarbiturate Derivatives as Effective Inhibitors of beta-glucuronidase. Journal of Ongoing Chemical Research, 4(1), 32-36. https://doi.org/10.5281/zenodo.3576583

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