ArticleBioMed research international2022
Cephalosporin as Potent Urease and Tyrosinase Inhibitor: Exploration through Enzyme Inhibition, Kinetic Mechanism, and Molecular Docking Studies.
Article in BioMed research international, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Review
- Identification and assessment of hub genes and miRNAs coregulatory associated with immune infiltrations and drug interactions in latent tuberculosis based on MicroarrayData analysis, molecular docking, and dynamic simulation.Biochemistry and biophysics reports · 2025Article
- Pyridylpiperazine-based carbodithioates as urease inhibitors: synthesis and biological evaluation.Frontiers in chemistry · 2024Article
- Zinc Oxide Nanoparticles Promise Anticancer and Antibacterial Activity in Ovarian Cancer.Pharmaceutical research · 2023Article
- Tyrosinase Inhibitors Naturally Present in Plants and Synthetic Modifications of These Natural Products as Anti-Melanogenic Agents: A Review.Molecules (Basel, Switzerland) · 2023Review
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Authors and funding
8 authors.
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Abstract
In present study, eleven cephalosporin drugs were selected to explore their new medically important enzyme targets with inherited safety advantage. To this end, selected drugs with active ingredient, cefpodoxime proxetil, ceftazidime, cefepime, ceftriaxone sodium, cefaclor, cefotaxime sodium, cefixime trihydrate, cephalexin, cefadroxil, cephradine, and cefuroxime, were evaluated and found to have significant activity against urease (IC50 = 0.06 ± 0.004 to 0.37 ± 0.046 mM) and tyrosinase (IC50 = 0.01 ± 0.0005 to 0.12 ± 0.017 mM) enzymes. Urease activity was lower than standard thiourea; however, tyrosinase activity of all drugs outperforms (ranging 6 to 18 times) the positive control: hydroquinone (IC50 = 0.18 ± 0.02 mM). Moreover, the kinetic analysis of the most active drugs, ceftriaxone sodium and cefotaxime sodium, revealed that they bind irreversibly with both the enzymes; however, their mode of action was competitive for urease and mixed-type, preferentially competitive for tyrosinase enzyme. Like
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