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The Interaction of Mastoparan B from Venom of a Hornet Vespa Basalis with Phospholipid Matrices
Park, Nam Gyu,Yamato, Yuhji,Lee, Sannamu,Sugihara, Gohsuke,Park, Jang-Su,Kang, Shin-Won 부산대학교 유전공학연구소 1996 분자생물학 연구보 Vol.12 No.-
Mastoparan B (MP-B) that is a novel MP isolated from the hornet Vespa basalis, was studied as compared with MP. in terms of interaction with phospholipid bilalyer and antimicrobial activity. MP-B has more hydrophilic amino acid residues in hydrophilic face of amphiphilic α-helical structure than MP. The both peptides exhibited considerably different effect on interaction with lipid bilayers, e.g. their conformation in the presence of acidic and neutral liposomes, cye-release ability from encapsulated liposomes, but on the whole the interaction mode was similar. On antimicrobial activity. MP had a strong activity against Gram-positive bacteria but no against Gram-negative ones. Since both peptides have almost same residues on the hydrophobic side, such more hydrophilic surface on the molecule seems to lead to the subtle change in its interaction with membranes, resulting in the alternation in its biological activity.
Conformation and Biological Activity of Mastoparan B and Its Analogs Ⅰ
Park, Nam Gyu,Seo, Jung-Kil,Ku, Hee-Jung,Lee, Sannamu,Sugihara, Gohsuke,Kim, Kwang-Ho,Park, Jang-Su,Kang, Shin-Won 부산대학교 유전공학연구소 1997 분자생물학 연구보 Vol.13 No.-
The mode of action of mastoparan B, an antimicrobial cartionic tetradecapeptide amide isolated from the hornet Vespa basails, toward phospholipid bilayers was studied with synthetic mastoparan B and its analogs with individual Ala instead of hydrophobic amino acids(1-Ile, 3-Leu,6-Leu,7-Val,9-Trp,13-Val,14-Leu)in mastoparan B. Mastoparan B and its analogs adopted an undered structure in buffer solution. In the preence of neutral and acidic liposomes, most of the peptides took an α-helical structure. The calcein leakage experiment indicated that mastoparan B interacted strongly with neutral and acidic lipid bilayers than its analogs. Mastoparan B also showed a more or less highly antimicrobial activity and hemolytic activitic for human erythrocytes than its analogs. These results indicate that the hydrophobic face in the amphipathic α-helix of mastoparan B critically affect biological activity and helical contents.
Interaction of Mastoparan B and Its Ala-Substituted Analogs with Phospholipid Bilayers
Park, Nam Gyu,Seo, Jung-Kil,Ku, Hee-Jung,Kim, Seung-Ho,Lee, Sannamu,Sugihara, Gohsuke,Kim, Kwang-Ho,Park, Jang-Su,Kang, Shin-Won 부산대학교 유전공학연구소 1997 분자생물학 연구보 Vol.13 No.-
The interaction of mastoparan B, a tetradecapeptide toxin found in the hornet Vespa basails, with phospholipid bilayers was investigated. Synthetic mastoparan B and its analogs,obstained 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 sythesized by the soild-phase method. As shown by circular dichroism spectra,mastoparan B and its analogs adopted an unordered structure in buffer solution. All paptides took an α-helical structure, and α-helical content of its analogs increased in the presebce 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.