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• W1971673313 abstract "We investigated the mechanism of candidacidal action of a Lys/Leu-rich α-helical model antimicrobial peptide (K9L8W) and its diastereomeric peptide (D9-K9L8W) composed of D,L-amino acids. K9L8W killed completely Candida albicans within 30 min, but D9-K9L8W killed only 72% of C. albicans even after 100 min. Tryptophan fluorescence spectroscopy indicated that the fungal cell selectivity of D9-K9L8W is closely correlated with a selective interaction with the negatively charged PC/PE/PI/ergosterol (5:2.5:2.5:1, w/w/w/w) phospholipids, which mimic the outer leaflet of the plasma membrane of C. albicans. K9L8W was able to induce almost 100% calcein leakage from PC/PE/PI/ergosterol (5:2.5:2.5:1, w/w/w/w) liposomes at a peptide:lipid molar ratio of 1:16, whereas D9-K9L8W caused only 25% dye leakage even at a peptide:lipid molar ratio of 1:2. Confocal laser-scanning microscopy revealed that FITC-labeled D9-K9L8W penetrated the cell wall and cell membrane and accumulated inside the cells, whereas FITC-labeled K9L8W did not penetrate but associated with the membranes. Collectively, our results demonstrated that the candidacidal activity of K9L8 W and D9-K9L8W may be due to the transmembrane pore/channel formation or perturbation of the fungal cytoplasmic membranes and the inhibition of intracellular functions, respectively. Finally, D9-K9L8W with potent anti-Candida activity but no hemolytic activity may be potentially a useful lead compound for the development of novel antifungal agents. Copyright © 2010 European Peptide Society and John Wiley & Sons, Ltd." @default.
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• W1971673313 date "2010-07-20" @default.
• W1971673313 modified "2023-10-16" @default.
• W1971673313 title "Candidacidal mechanism of a Leu/Lys-rich α-helical amphipathic model antimicrobial peptide and its diastereomer composed of D ,L -amino acids" @default.
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• W1971673313 doi "https://doi.org/10.1002/psc.1268" @default.
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