• 한국환경과학회지
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• 제6권2호
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• pp.189-194
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• 1997

Hornet venom의 독성 peptide인 mastoparan과 mastoparan-B를 solid phase peptide syn- thesis method로 합성한 후 이들과 phospholipid와의 상호작용, 이들의 항균 활성 및 용혈 활성 을 조사하였다. 두가지 독성 peptide 모두 중성 liposome에서 저 농도에서도 dye release를 유도할 수 있었다. 중성 liposome에 대한 mastoparan-B의 결합 친화도는 산성 liposome에서 보다 작았다. Mastoparan과 mastoparan-B는 두가지 모두 그람 양성 세균에 대하여 강한 항균 활성을 가지고 있었으나 그람 음성 세균에 대해서는 각각 약하거나 유력한 활성을 보였다. Mastoparan과 mastoparan-B는 5$\mu$M의 낮은 농도에서도 적혈구를 분해시키는 독성을 보였다.

• Bulletin of the Korean Chemical Society
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• 제18권9호
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• pp.933-938
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• 1997

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.

• Bulletin of the Korean Chemical Society
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• 제18권1호
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• pp.50-56
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• 1997

The mode of action of mastoparan B, an antimicrobial cationic tetradecapeptide amide isolated from the hornet Vespa basalis, 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 were synthesized by the solid-phase method. Circular dichroism spectra showed that mastoparan B and its analogs adopted an unordered structure in buffer solution. In the presence 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 activity 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.

• 한국환경과학회지
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• 제12권1호
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• pp.77-80
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• 2003

The interaction of mastoparan B, a cationic tetradecapeptide amide isolated from the hornet Vespa basalis, with phospholipid bilayers was studied with synthetic mastoparan B and its analogue with Ala instead of hydrophobic 12th amino acid residue in mastoparan B. MP-B and its derivative, [12-Ala]MP-B were synthesized by the solid-phase peptide synthesis method. MP-B and its analogue, [12-Ala]MP-B adopted an unordered structure in buffer solution. In the presence of neutral and acidic liposomes, the peptides took an $\alpha$-helical structure. The two peptides interacted with neutral and acidic lipid bilayers. These results indicated that the hydrophobic face in the amphipathic $\alpha$-helix of MP-B critically affected the biological activity and helical content.

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 1999년도 학술발표회 진행표 및 논문초록
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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)

• 한국어병학회지
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• 제16권3호
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• pp.193-201
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• 2003

Mastoparan B (MPB)는 벌독으로부터 정제된 양친매성 $\alpha$-helical 구조를 취하면서 14개의 아미노산 잔기로 구성된 염기성 항균성 펩타이드로서 여러가지 생물막과 작용한다. 본 연구에서는 우리 나라 연안의 적조 (HABs, harmful algal blooms)를 일으키는 4종의 적조생물 (Alexandrium tamarense, Chattonella marina, Cochlodinium polykrikoides 및 Gymnodinium catenatum)에 대한 MPB의 살조효과를 조사하였다. MPB의 4종의 적조생물에 대한 살조효과는 31.3 $\mu{g}$/mL부터 500 $\mu{g}$/mL에서 세포의 lysis 또는 ecdysis와 같은 형태로 현미경으로 관찰할 수 있었다. 또한 MPB는 C. marina 및 C. polykrikorides에 대해서 A. tamarense와 G. catenatum보다 더욱 강한 살조효과를 나타내었다. 이러한 MPB의 HABs에 대한 살조효과연구는 새로운 살조물질을 개발하기 위한 자료가 될 것으로 생각된다.

• 미생물학회지
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• 제34권1_2호
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• pp.26-30
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• 1998

Tetradecapeptide인 Mastoparan B(MP B)와 이의 [Ala]-MP B 유도체들을 합성하고 항균 활성 및 용혈 작용을 측정하여 MP B의 활성에 미치는 소수성도(hydrophobicity)와 양친매성(amphiphilicity)의 영향을 비교하였다. 그 결과 MP B와 소수성도가 MP B 보다 큰 [$Ala^2$]-, [$Ala^4$]-MP B 유도체가 큰 항균 활성을 나타내었으며, 소수성도가 MP B보다 작은 [$Ala^6$]-MP B 유도체의 활성은 MP B와 비슷하거나 작게 나타나 소수성도가 큰 유도체일수록 항균 활성을 크게 나타내었다. 그러나 MP B 보다 소수성도가 큰 유도체인 [$Ala^9$]-MP B는 Ala에 의한 Trp의 치환때문에 MP B 보다 작은 활성을 나타내었다. 용혈 활성 측정 결과 MP B보다 소수성도가 큰 [$Ala^2$]-, [$Ala^4$]-MP B 유도체가 각각 100.0%와 69.4%로써 용혈 작용을 크게 나타냈으나, 소수성도가 작은 [$Ala^6$]-MP B 유도체는 6.1%로써 가장 작은 용혈 작용을 나타내었고 Trp 대신 Ala으로 치환한 소수성도가 큰 유도체인 [$Ala^9$]-MP B는 MP B 보다 작은 26.0%의 용혈 작용을 나타내었다. 그러므로 용혈 작용은 소수성도가 클수록 증가하였으며 양친매성이 활성에 미치는 영향은 적었다.

• 한국동물위생학회지
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• 제42권4호
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• pp.257-264
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• 2019

Mastoparan V1 was used as adjuvant of formalin-inactivated Salmonella Gallinarum whole cells vaccine against fowl typhoid in a chicken model. The 75 brown nick chickens were equally divided into 5 groups, and all chickens of each group were immunized at 6 weeks of age (0 WPPI; weeks prime post immunization), and at 9 weeks of age (3 WPPI) (except group B). Group A chickens were intramuscularly (IM) inoculated with 500 uL of sterile phosphate-buffered saline (PBS), and group B chickens were subcutaneously immunized with 0.2 ml containing 5×10⁷ viable vaccine strain/bird. The chickens in groups C~E were IM inoculated with approximately 3×10⁹ cells/0.5 mL of formalin-inactivated the S. Gallinarum whole cells, approximately 3×10⁹ cells/0.5 mL of formalin-inactivated the S. Gallinarum whole cells with mastoparan V1 as adjuvant, and 0.5 mL of PBS, respectively. S. Gallinarum outer membrane proteins-specific serum IgG titers were considerably higher in groups B~D than in groups A and E. However, the levels of IFN-γ in groups B and D only than in groups A and E were significantly higher. Following oral challenge with virulent wild-type S. Gallinarum, no chicken in groups A (no challenge group) and B was dead, and only 30% of chickens in group D was dead. However, 70% of chickens in group C and all chickens in group E were dead after oral challenge. The results of this study demonstrated that IM immunization with approximately 3×10⁹ of the formalin-inactivated S. Gallinarum whole cells containing mastoparan V1 induced robust antibody and cell-mediated immune responses in chickens. The whole cells also conferred protection against infection with wild-type S. Gallinarum.

• Bulletin of the Korean Chemical Society
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• 제17권3호
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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.

• 한국자기공명학회:학술대회논문집
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• 한국자기공명학회 1999년도 하계총회 및 제15회 자기공명 학술발표회
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• pp.30-30
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• 1999