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- W2023277847 abstract "A 25-mer cationic peptide pleurocidin, isolated from the winter flounder, has broad antibacterial activity. To clarify the structure-activity relationship, its properties and biological activity were examined. CD measurements showed that pleurocidin took an alpha-helical structure in the presence of DOPC/DOPG (3:1, anionic) vesicles. Very weak hemolytic activity of pleurocidin was observed and its antibacterial activity was moderate. Tryptophan fluorescence shift measurements showed that pleurocidin interacted weakly with a neutral phospholipid, but strongly with an acidic phospholipid. The peptide exhibited weak dye-leakage activity for DOPC (neutral) vesicles and moderate activity for acidic vesicles. From experiments on dye-leakage activity and membrane translocation of the peptide, it seemed likely that pleurocidin, like magainin 2, forms pores in the lipid membrane. A study of amino acid substitution in pleurocidin revealed that alpha-helicity, rather than hydrophobicity, affects the properties and activity of the peptide." @default.
- W2023277847 created "2016-06-24" @default.
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- W2023277847 date "2001-02-01" @default.
- W2023277847 modified "2023-09-27" @default.
- W2023277847 title "Interaction of pleurocidin and its analogs with phospholipid membrane and their antibacterial activity" @default.
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- W2023277847 doi "https://doi.org/10.1034/j.1399-3011.2001.00802.x" @default.
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