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• W2138616658 abstract "The fungicidal effects of the peptide HP (2-20). derived from the N-terminal sequence of Helicobacter pylori ribosomal protein L1 (RPL1). have been investigated. HP (2-20) displays a strong fungicidal activity against various fungi, without haemolytic activity against human erythrocyte cells, and the fungicidal activity is inhibited by Ca2+ and Mg2+ ions. In order to investigate the fungicidal mechanism(s) of HP (2-20). the amount of intracellular trehalose was measured in C. albicans. It was found that the amounts of intracellular trehalose were decreased when HP (2-20) was used. The action of the peptide against fungal cell membranes was further examined by the potassium-release test; HP (2-20) was found to increase the amount of K+ released from the cells. Furthermore, HP (2-20) caused significant morphological changes, as shown by scanning electron microscopy, and by testing the membrane disrupting activity using liposomes (phosphatidyl choline/cholesterol; 10: 1, w/w). Our results suggest that HP (2-20) may exert its antifungal activity by disrupting the structure of cell membranes, via pore formation or direct interaction with the lipid bilayers." @default.
• W2138616658 created "2016-06-24" @default.
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• W2138616658 date "2002-01-01" @default.
• W2138616658 modified "2023-10-18" @default.
• W2138616658 title "HP (2-20) derived from the amino terminal region ofHelicobacter pylori ribosomal protein L1 exerts its antifungal effects by damaging the plasma membranes ofCandida albicans" @default.
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• W2138616658 doi "https://doi.org/10.1002/psc.405" @default.
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