Synthetic antimicrobial peptides of the halictines family disturb the membrane integrity of Candida cells
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F17%3A00476797" target="_blank" >RIV/67985823:_____/17:00476797 - isvavai.cz</a>
Výsledek na webu
<a href="http://dx.doi.org/10.1016/j.bbamem.2017.06.005" target="_blank" >http://dx.doi.org/10.1016/j.bbamem.2017.06.005</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.bbamem.2017.06.005" target="_blank" >10.1016/j.bbamem.2017.06.005</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Synthetic antimicrobial peptides of the halictines family disturb the membrane integrity of Candida cells
Popis výsledku v původním jazyce
We compared the potency of four derivatives of the antimicrobial peptide halictine-2 against six Candida species. Observed activity was peptide and species specific. Halictines rapidly permeabilized cell membranes and caused the leakage of cytosolic components. Their killing potential was enhanced by the commercial antimicrobial agent octenidine dihydrochloride. The effect on C. glabrata cells did not depend on the activity of Cdr pumps, but was influenced by their lipid composition. The pre-treatment of cells with myriocin, an inhibitor of sphingolipid synthesis, enhanced the peptides' activity, whereas pre-treatment with terbinafine and fluconazole, inhibitors of sterol synthesis, significantly weakened their efficacy. The killing efficacy of peptides increased in combination with amphotericin B. Thus the mode of action of halictines is likely to depend on the plasma-membrane sterols, which might explain the observed differences among the tested Candida species.
Název v anglickém jazyce
Synthetic antimicrobial peptides of the halictines family disturb the membrane integrity of Candida cells
Popis výsledku anglicky
We compared the potency of four derivatives of the antimicrobial peptide halictine-2 against six Candida species. Observed activity was peptide and species specific. Halictines rapidly permeabilized cell membranes and caused the leakage of cytosolic components. Their killing potential was enhanced by the commercial antimicrobial agent octenidine dihydrochloride. The effect on C. glabrata cells did not depend on the activity of Cdr pumps, but was influenced by their lipid composition. The pre-treatment of cells with myriocin, an inhibitor of sphingolipid synthesis, enhanced the peptides' activity, whereas pre-treatment with terbinafine and fluconazole, inhibitors of sterol synthesis, significantly weakened their efficacy. The killing efficacy of peptides increased in combination with amphotericin B. Thus the mode of action of halictines is likely to depend on the plasma-membrane sterols, which might explain the observed differences among the tested Candida species.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10606 - Microbiology
Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2017
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Biochimica Et Biophysica Acta-Biomembranes
ISSN
0005-2736
e-ISSN
—
Svazek periodika
1859
Číslo periodika v rámci svazku
10
Stát vydavatele periodika
NL - Nizozemsko
Počet stran výsledku
8
Strana od-do
1851-1858
Kód UT WoS článku
000411419000010
EID výsledku v databázi Scopus
2-s2.0-85024090021