Cephalosporin as Potent Urease and Tyrosinase Inhibitor: Exploration through Enzyme Inhibition, Kinetic Mechanism, and Molecular Docking Studies.
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, cefixi...
| Publicado en: | BioMed Research International pp. 1 - 12 |
|---|---|
| Autores principales: | , , , , , , , |
| Formato: | research tables/charts Journal Article |
| Publicado: |
Wiley-Blackwell
7/28/2022
|
| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=ccm&AN=158239225&site=ehost-live header: @attributes: shortDbName: ccm uiTerm: 158239225 longDbName: CINAHL Complete uiTag: AN controlInfo: bkinfo: dissinfo: jinfo: jid: 23146133 FT2T jtl: BioMed Research International issn: 23146133 maglogo: N pubinfo: dt: 7/28/2022 pid: 480 pub: Wiley-Blackwell place: Malden, Massachusetts artinfo: ui: 158239225 158239225 158239225 10.1155/2022/1092761 158239225 ppf: 1 ppct: 11 formats: fmt: – @attributes: type: T – @attributes: type: P tig: atl: Cephalosporin as Potent Urease and Tyrosinase Inhibitor: Exploration through Enzyme Inhibition, Kinetic Mechanism, and Molecular Docking Studies. aug: au: Alqahtani, Yahya S. Alyami, Bandar A. Alqarni, Ali O. Mahnashi, Mater H. Ali, Anser Javed, Qamar Hassan, Mubashir Ehsan, Muhammad affil: Department of Pharmaceutical Chemistry, College of Pharmacy, Najran University, Najran, Saudi Arabia sug: subj: Cephalosporins Therapeutic Use Urease Therapeutic Use Enzyme Inhibitors Therapeutic Use Molecular Docking Simulation Safety Human Cefaclor Cefotaxime Cefepime Hydrochloride Antibiotics Oxidoreductases Phenols Kinetics Ceftriaxone Enzymes In Vitro Studies ab: 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 (IC 50 = 0.06 ± 0.004 to 0.37 ± 0.046 mM) and tyrosinase (IC 50 = 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 (IC 50 = 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 in vitro activity, ceftriaxone sodium and cefotaxime sodium docking analysis showed their considerable binding affinity and significant interactions with both urease and tyrosinase enzymes sufficient for downstream signaling responsible for observed enzyme inhibition in vitro, purposing them as potent candidates to control enzyme-rooted obstructions in future. pubtype: Academic Journal doctype: research tables/charts Journal Article ougenre: Article language: English refInfo: holdings: @attributes: islocal: N |
|---|