Synthetic antimicrobial peptides of the halictines family disturb the membrane integrity of Candida cells

0476797 - FGÚ 2018 RIV NL eng J - Journal Article
Kodedová, Marie - Sychrová, Hana
Synthetic antimicrobial peptides of the halictines family disturb the membrane integrity of Candida cells.
Biochimica Et Biophysica Acta-Biomembranes. Roč. 1859, č. 10 (2017), s. 1851-1858. ISSN 0005-2736. E-ISSN 1879-2642
R&D Projects: GA TA ČR(CZ) TA04010638; GA ČR(CZ) GA16-03398S; GA MŠMT(CZ) LQ1604; GA MŠMT(CZ) ED1.1.00/02.0109
Institutional support: RVO:67985823
Keywords : antimicrobial peptide * Candida * diS-C3(3) assay * membrane potential * membrane lipids * halictine
OECD category: Microbiology
Impact factor: 3.438, year: 2017

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.
Permanent Link: http://hdl.handle.net/11104/0273210