Cited 0 time in
- Title
- Interaction of mastoparan B and its ala-substituted analogs with phospholipid bilayers
- Author(s)
- 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
- 1997
- Abstract
- 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.
- ISSN
- 0253-2964
- Publisher
- Wiley
- Type
- Article
- Appears in Collections:
- 1. Journal Articles > Journal Articles
- Files in This Item:
Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.