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Inhibition of urease by urea/thiourea-derived heterocycles: IC50 profiling and structure-activity relationship.

Bibliographic Details
Title: Inhibition of urease by urea/thiourea-derived heterocycles: IC50 profiling and structure-activity relationship.
Authors: Bağ A; Institute of Science, Kafkas University, 36100, Kars, Turkey., Uluçay O; Department of Bioengineering, Faculty of Engineering and Architecture, Kafkas University, 36100, Kars, Turkey. Electronic address: orhanulucay@gmail.com.
Source: Biochimie [Biochimie] 2026 Jun; Vol. 245, pp. 160-167. Date of Electronic Publication: 2026 Mar 23.
Publication Type: Journal Article
Language: English
Journal Info: Publisher: Editions Scientifiques Elsevier Country of Publication: France NLM ID: 1264604 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1638-6183 (Electronic) Linking ISSN: 03009084 NLM ISO Abbreviation: Biochimie Subsets: MEDLINE
Imprint Name(s): Publication: Paris : Editions Scientifiques Elsevier
Original Publication: Paris.
MeSH Terms: Urease*/antagonists & inhibitors , Urease*/chemistry , Thiourea*/chemistry , Enzyme Inhibitors*/chemistry , Enzyme Inhibitors*/pharmacology , Urea*/chemistry , Heterocyclic Compounds*/chemistry , Heterocyclic Compounds*/pharmacology, Canavalia/enzymology ; Structure-Activity Relationship ; Inhibitory Concentration 50
Abstract: The urease enzyme catalyzes the hydrolysis of urea and plays a critical role in both agricultural and clinical contexts, contributing to nitrogen loss from urea-based fertilizers and promoting the survival and virulence of urease-positive pathogens such as Helicobacter pylori. Therefore, urease inhibitors are considered valuable targets for environmental and therapeutic applications. In this study, the in vitro urease inhibition potentials of five-membered heterocyclic compounds derived from thiourea were investigated. A comparative evaluation was performed using thiourea as the standard inhibitor. Using the Weatherburn indophenol method, IC50 values were calculated from concentration-dependent inhibition curves. The results revealed that all compounds exhibited significant inhibition at low micromolar levels. Specifically, 2-thiohydantoin (IC50 = 2.47 μM) and hydantoin (IC50 = 2.62 μM) were identified as the most potent inhibitors, while rhodanine (IC50 = 3.46 μM) and creatinine (IC50 = 3.63 μM) exhibited moderate effects. 2,4-thiazolidinedione (IC50 = 3.77 μM) was found to be relatively weaker. Compared to the standard inhibitor thiourea (IC50 = 3.67 μM), most of the tested compounds showed similar or higher activity. The results indicate that replacing the CO group with CS can enhance inhibitory activity. Structural differences were also found to play a decisive role in enzyme ligand interactions. This study demonstrates the potential of thiourea-derived heterocyclic scaffolds as effective urease inhibitors.
(Copyright © 2026 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.)
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
Contributed Indexing: Keywords: Heterocyclic compounds; IC(50); Inhibition; Thiourea; Urease
Substance Nomenclature: EC 3.5.1.5 (Urease)
GYV9AM2QAG (Thiourea)
0 (Enzyme Inhibitors)
8W8T17847W (Urea)
0 (Heterocyclic Compounds)
Entry Date(s): Date Created: 20260325 Date Completed: 20260713 Latest Revision: 20260713
Update Code: 20260714
DOI: 10.1016/j.biochi.2026.03.009
PMID: 41881276
Database: MEDLINE
Description
ISSN:1638-6183
DOI:10.1016/j.biochi.2026.03.009