• Title/Summary/Keyword: hornet venom

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Bioenvironmental Interaction of Toxic Peptide Hornet Venom with Phospholipid (Hornet 독액의 독성 Peptide와 Phospholipid 간의 생체환경적 상호작용)

  • 김광호;이봉헌
    • Journal of Environmental Science International
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    • v.6 no.2
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    • pp.189-194
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    • 1997
  • Toxic peptides from hornet venom, mastoparan and mastoparan-B were synthesized us- ing the solid phase peptide synthesis method and investigated the interaction of them with phospholipid bilayer, antibacterial activity, and hemolytic activity. Both toxic peptides could induce dye release at a low concentration in neutral liposome. The binding affinity of mastoparan-B for neutral liposome was smaller than that for acidic one. Mastoparan and mastoparan-B had strong antibacterial activity for gram-positive bacteria, but weak or potent activity for gram-negative ones, respectively. Mastoparan and mastoparan-B lysed erythrocyte very little up to 5 $\mu$M.

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Interaction of Hornet Venom and its Derivatives in the Phospholipid Membrane Environment (말벌 독성 물질과 그 유도체의 인지질 막 환경에서의 상호작용)

  • 이봉헌;박홍재
    • Journal of Environmental Science International
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    • v.7 no.1
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    • pp.62-66
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    • 1998
  • Toxic Mastoparan B(MP-B) which is purified from the venom of the hornet Vespa basalis is a cationic amphlphilic tetradecapeptide. MP-B and Its Ala-substituted analogues were synthesized by solld phase method and the toxic peptide-membrane interactions were examined by circular dichroism(CD) spectra, fluorescence spectra, and leakage abilities in phospholipid membranes. In the presence of phospholipid vesicles, synthetic MP-B and its analogues formed amphiphilic -helical structures, but in the buffer soletion, those exhibited random coil conformation as measured by CD. Fluorescence spectra of MP-B and its analogues which indicated the binding affinity of peptide on phospholipid vesicles showed that the replacement of Lys at position 2 and 11 with Ala caused a remarkable effect in the blue shalt and that at position 2, in the leakage ability of the peptide.

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The Interaction of Mastoparan B from Venom of a Hornet Vespa Basalis with Phospholipid Matrices

  • 박남규;Yuhji Yamato;Sannamu Lee;Gohsuke Sugihara;박장수;강신원
    • Bulletin of the Korean Chemical Society
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    • v.17 no.3
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    • pp.239-244
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    • 1996
  • 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 bilayer 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, dye-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. Contrary to this, MP-B had a strong activity against Gram-positive and potent 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.

Studies of Tertiary Structures of Mastoparan B and Alanine Analogues by NMR Spectroscopy

  • Kyeunghee Yu;Kang, Shin-Won;Park, Nam-Gyu;Kim, Yangmee
    • Proceedings of the Korean Biophysical Society Conference
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    • 1999.06a
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    • pp.33-33
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    • 1999
  • Mastoparan B (MP-B), an antimicrobial cationic tetradecapeptide amide isolated from the venom of the hornet Vespa basalis, is an amphiphilic ${\alpha}$-helical peptide. In order to study the relationship between the structure and biological activity, we used the three analogues by replacing amino acids with alanine (4LysAla: 4MP-B, 12-LYsAla: 12MP-B, 9TrpAla: 9Mp-B).(omitted)

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The Algicidal Effect of Antimicrobial Peptide, Mastoparan B (항균성 펩타이드인 mastoparan B의 살조효과)

  • Seo, Jeong-Gil;Kim, Chan-Hui;Bae, Yun-Jeong;Mun, Ho-Seong;Kim, Geun-Yong;Park, Hui-Yeon;Yun, Ho-Dong;Kim, Chang-Hun;Byeon, Dae-Seok;Hong, Yong-Gi;Park, Nam-Gyu
    • Journal of fish pathology
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    • v.16 no.3
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    • pp.193-201
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    • 2003
  • Mastoparan B (MPB), an antimicrobial cationic peptide isolated from the venom of the hornet Vespa basalis, is a basic amphipathic α-helical peptide composed of fourteen amino acid residues. In this study, we have investigated the algicidal effect of MPB against harmful algae blooms (HABs) casative Alexandrium tamarense, Chattonella marina, Cochlodinium polykrikoides and Gymnodinium catenatum. The algicidal effect of MPB showed in the concentration of 31.3 $\mu{g}$/mL to 500 $\mu{g}$/mL against 4 HAB species and observed cell lysis or cell ecdysis by microscopy. MPB reacted more sensitive to C. marina and C. polykrikoides than A. tamarense and G. catenatum. The algicidal study of MPB against HABs will provides much insight into development of new algicidal substances.