Non-target biotransformation enzymes as a target for triazole-zinc mixtures
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F23%3A00574688" target="_blank" >RIV/61388971:_____/23:00574688 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/60460709:41210/23:94804 RIV/00216208:11310/23:10465865 RIV/00216208:11510/23:10465865
Výsledek na webu
<a href="https://www.sciencedirect.com/science/article/pii/S0009279723002922?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S0009279723002922?via%3Dihub</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.cbi.2023.110625" target="_blank" >10.1016/j.cbi.2023.110625</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Non-target biotransformation enzymes as a target for triazole-zinc mixtures
Popis výsledku v původním jazyce
Triazoles inhibit lanosterol 14 & alpha,-demethylase and block ergosterol biosynthesis in fungal pathogens. However, they also interact with other cytochrome P450 enzymes and influence non-target metabolic pathways. Disturbingly, triazoles may interact with essential elements. The interaction of penconazole (Pen), cyproconazole (Cyp) and tebuconazole (Teb) with Zn2+ results in the formation of deprotonated ligands in their complexes or in the creation of complexes with Cl- as a counterion or doubly charged complexes. Triazoles, as well as their equimolar cocktails with Zn2+ (10-6 mol/L), decreased the activities of the non-target enzymes CYP19A1 and CYP3A4. Pen most decreased CYP19A1 activity and was best bound to its active centre to block the catalytic cycle in computational analysis. For CYP3A4, Teb was found to be the most effective inhibitor by both, activity assay and interaction with the active centre. Teb/Cyp/Zn2+ and Teb/Pen/Cyp/Zn2+ cocktails also decreased the CYP19A1 activity, which was in correlation with the formation of numerous triazole-Zn2+ complexes.
Název v anglickém jazyce
Non-target biotransformation enzymes as a target for triazole-zinc mixtures
Popis výsledku anglicky
Triazoles inhibit lanosterol 14 & alpha,-demethylase and block ergosterol biosynthesis in fungal pathogens. However, they also interact with other cytochrome P450 enzymes and influence non-target metabolic pathways. Disturbingly, triazoles may interact with essential elements. The interaction of penconazole (Pen), cyproconazole (Cyp) and tebuconazole (Teb) with Zn2+ results in the formation of deprotonated ligands in their complexes or in the creation of complexes with Cl- as a counterion or doubly charged complexes. Triazoles, as well as their equimolar cocktails with Zn2+ (10-6 mol/L), decreased the activities of the non-target enzymes CYP19A1 and CYP3A4. Pen most decreased CYP19A1 activity and was best bound to its active centre to block the catalytic cycle in computational analysis. For CYP3A4, Teb was found to be the most effective inhibitor by both, activity assay and interaction with the active centre. Teb/Cyp/Zn2+ and Teb/Pen/Cyp/Zn2+ cocktails also decreased the CYP19A1 activity, which was in correlation with the formation of numerous triazole-Zn2+ complexes.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10606 - Microbiology
Návaznosti výsledku
Projekt
—
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2023
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Chemico-Biological Interactions
ISSN
0009-2797
e-ISSN
1872-7786
Svazek periodika
382
Číslo periodika v rámci svazku
1 September
Stát vydavatele periodika
IE - Irsko
Počet stran výsledku
8
Strana od-do
110625
Kód UT WoS článku
001039350600001
EID výsledku v databázi Scopus
2-s2.0-85164817854