Thiosemicarbazone Derivatives Act As Potent Urease Inhibitors; Synthesis, Bioactivity Screening and Molecular Docking Study

Thiosemicarbazone Derivatives Act As Potent Urease Inhibitors; Synthesis, Bioactivity Screening and Molecular Docking Study Publisher

Moghadam ES¹ ; Alsadi AM² ; Talebi M³ ; Amanlou M^{3, 4} ; Stoll R⁵ ; Amini M^{3, 4} ; Abdeljalil R¹

Show Affiliations

1. Department of Chemistry, College of Science, Sultan Qaboos University, P.O. Box 36, Muscat, P.C. 123, Oman
2. Department of Crop Sciences, College of Agricultural and Marine Sciences, Sultan Qaboos University, Muscat, Oman
3. Department of Medicinal Chemistry, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, 1417614411, Iran
4. Drug Design and Development Research Center, The Institute of Pharmaceutical Sciences (TIPS), Tehran University of Medical Sciences, Tehran, Iran
5. Biomolecular NMR, Ruhr University of Bochum, Bochum, D-44780, Germany

Source: ChemistrySelect Published:2022

Abstract

An enzyme called urease assists highly pathogenic bacteria in colonizing and maintaining themselves. Accordingly, inhibiting urease enzymes has been shown to be a promising strategy for preventing ureolytic bacterial infections. So, design and synthesis of potent and safe urease inhibitors converted to an interesting target for medicinal chemists. In this study, the design, synthesis, and bioactivity of fourteen thiosemicarbazone derivatives 5 a–n are described as potent urease inhibitors. A variety of spectroscopic techniques (1H-NMR, 13C-NMR, MS), and elemental analysis were utilized to determine the structure of 5 a–n. Interestingly, all 5 a–n showed higher inhibitory activity (IC50: 4.08 to 11.31 μM) than the standards thiourea and hydroxyurea (IC50: 22 and 100 μM respectively). 5 g and 5 f exhibited the best activity with IC50 values of 4.08 and 4.79 μM, respectively. Molecular docking was also used to reveal the potential interactions between the enzyme‘s active site and the most active compound. An MTT assay was conducted on two different cell lines to investigate the cytotoxic effect of the tested compounds. all 5 a–n have IC50 values above 50 μM on both tested cell lines. In conclusion, current reported compounds are potent and safe enough to continue further bioassays to find a new drug candidate. © 2022 Wiley-VCH GmbH.

Style	Citing Format
MLA	Moghadam ES, et al.. "Thiosemicarbazone Derivatives Act As Potent Urease Inhibitors; Synthesis, Bioactivity Screening and Molecular Docking Study." ChemistrySelect, vol. 7, no. 23, 2022, pp. -.
APA	Moghadam ES, Alsadi AM, Talebi M, Amanlou M, Stoll R, Amini M, Abdeljalil R (2022). Thiosemicarbazone Derivatives Act As Potent Urease Inhibitors; Synthesis, Bioactivity Screening and Molecular Docking Study. ChemistrySelect, 7(23), -.
Chicago	Moghadam ES, Alsadi AM, Talebi M, Amanlou M, Stoll R, Amini M, Abdeljalil R. "Thiosemicarbazone Derivatives Act As Potent Urease Inhibitors; Synthesis, Bioactivity Screening and Molecular Docking Study." ChemistrySelect 7, no. 23 (2022): -.
Harvard	Moghadam ES et al. (2022) 'Thiosemicarbazone Derivatives Act As Potent Urease Inhibitors; Synthesis, Bioactivity Screening and Molecular Docking Study', ChemistrySelect, 7(23), pp. -.
Vancouver	Moghadam ES, Alsadi AM, Talebi M, Amanlou M, Stoll R, Amini M, et al.. Thiosemicarbazone Derivatives Act As Potent Urease Inhibitors; Synthesis, Bioactivity Screening and Molecular Docking Study. ChemistrySelect. 2022;7(23):-.
BibTex	@article{ author = {Moghadam ES and Alsadi AM and Talebi M and Amanlou M and Stoll R and Amini M and Abdeljalil R}, title = {Thiosemicarbazone Derivatives Act As Potent Urease Inhibitors; Synthesis, Bioactivity Screening and Molecular Docking Study}, journal = {ChemistrySelect}, volume = {7}, number = {23}, pages = {-}, year = {2022} }
RIS	TY - JOUR AU - Moghadam ES AU - Alsadi AM AU - Talebi M AU - Amanlou M AU - Stoll R AU - Amini M AU - Abdeljalil R TI - Thiosemicarbazone Derivatives Act As Potent Urease Inhibitors; Synthesis, Bioactivity Screening and Molecular Docking Study JO - ChemistrySelect VL - 7 IS - 23 SP - EP - PY - 2022 ER -

Science Communicator Platform

Authors

Authors Affiliations

Abstract