Interaction of mastoparan B and its ala-substituted analogs with phospholipid bilayers

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Interaction of mastoparan B and its ala-substituted analogs with phospholipid bilayers
Nam Gyu Park; Jung-Kil Seo; Hee-Jung Ku; Seung Ho Kim; Sannamu Lee; Gohsuke Sugihara; Kwang-Ho Kim; Jang-Su Park; Shin-Won Kang
Bibliographic Citation
Bulletin of Korean Chemical Society, vol. 18, no. 9, pp. 933-938
Publication Year
The interaction of mastoparan B, a tetradecapeptide toxin found in the hornet Vespa basalis, with phospholipid bilayers was investigated. Synthetic mastoparan B and its analogs, obtained by substituting one hydrophilic amino acid (2-Lys, 4-Lys, 5-Ser, 8-Ser, 11-Lys, or 12-Lys) in mastoparan B with Ala, were studied. Mastoparan B and its analogs were synthesized by the solid-phase method. As shown by circular dichroism spectra, mastoparan B and its analogs adopted an unordered structure in buffer solution. All peptides took an α-helical structure, and the α-helical content of its analogs increased in the presence of neutral and acidic liposomes as compared to that of mastoparan B. In the calcein leakage experiment, we observed that mastoparan B interacted more weakly with lipid bilayers in neutral and acidic media than its analogs. Mastoparan B also showed slightly lower antimicrobial activity and hemolytic activity towards human erythrocytes than its analogs. These results indicate that the greater hydrophobicity of the amphiphilic α-helix of mastoparan B by replacement with alamine residues results in the increased biological activity and helical content.
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