Release of aqueous contents from phospholipid vesicles induced by cecropin A (1-8)-magainin 2 (1-12) hybrid and its analogues

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dc.contributor.authorJ H Kang-
dc.contributor.authorSong Yub Shin-
dc.contributor.authorSo Youn Jang-
dc.contributor.authorMyung Kyu Lee-
dc.contributor.authorKyung Soo Hahm-
dc.description.abstractThe membrane-disrupting properties of cecropin A (1-8)-magainin 2 (1- 12) hybrid peptide, which has higher antitumor with less hemolytic activities than cecropin A (1-8)melittin (1-12), and its analogues were assessed by measuring the induced release of vesicle-entrapped fluorescence probes. A model membrane was made of zwitterionic phospholipid (phosphatidylcholine) or the mixture of negatively and zwitterionic phospholipids (phosphatidylcholine and phosphatidylserine). The extent of leakage of the aqueous content of the phospholipid vesicles was found to have remarkable discrepancies according to the amphipathic nature of each analogue peptide. The entrapped high molecular weight solute (fluorescein-labeled immunoglobulin G, 55 kDa) also was released by the analogue which had the largest hydrophobic region and the highest amphipathic score among peptides tested. As the result of the determination of the relationships between the membrane-disrupting properties and the hydrophobicity values of peptides, it was found that the membrane- disrupting activity increased according to increasing the hydrophobicity of the peptide. The tryptophan fluorescence emission spectra and CD spectra showed that on interaction with the phospholipid vesicle, the peptide acquired the ordered structure and α-helical conformation by moving a tryptophan residue into the nonpolar environment of the phospholipid vesicle. These results suggest that the breakdown of the lipid bilayer was mediated by the α-helical amphipathic structure of the peptide interacting with the lipid bilayers as well as the by the hydrophobicity of the peptide.-
dc.titleRelease of aqueous contents from phospholipid vesicles induced by cecropin A (1-8)-magainin 2 (1-12) hybrid and its analogues-
dc.title.alternativeRelease of aqueous contents from phospholipid vesicles induced by cecropin A (1-8)-magainin 2 (1-12) hybrid and its analogues-
dc.citation.titleChemical Biology & Drug Design-
dc.contributor.affiliatedAuthorJ H Kang-
dc.contributor.affiliatedAuthorSong Yub Shin-
dc.contributor.affiliatedAuthorSo Youn Jang-
dc.contributor.affiliatedAuthorMyung Kyu Lee-
dc.contributor.affiliatedAuthorKyung Soo Hahm-
dc.identifier.bibliographicCitationChemical Biology & Drug Design, vol. 52, pp. 45-50-
dc.subject.keywordcircular dichroism-
dc.subject.keywordfluorescence spectra-
dc.subject.keywordhybrid peptides-
dc.subject.keywordphospholipid vesicle-disrupting activities-
dc.subject.localcircular dichroism-
dc.subject.localCircular dichroism-
dc.subject.localfluorescence spectra-
dc.subject.localhybrid peptides-
dc.subject.localphospholipid vesicle-disrupting activities-
dc.subject.localphospholipid vesicle-disrupting activity-
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