• 제목/요약/키워드: magainin-2

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Effect of Cholesterol on the Phase Change of Lipid Membranes by Antimicrobial Peptides

  • Choi, Hyungkeun;Kim, Chul
    • Bulletin of the Korean Chemical Society
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    • 제35권5호
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    • pp.1317-1322
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    • 2014
  • Membrane disruption by an antimicrobial peptide (AMP) was investigated by measuring the $^2H$ solid-state nuclear magnetic resonance spectra of 1-palmitoyl-$d_{31}$-2-oleoyl-sn-glycero-3-phosphatidylcholine (POPC_$d_{31}$) in mixtures of POPC_$d_{31}$/cholesterol and either magainin 2 or aurein 3.3 deposited on thin cover-glass plates. The line shapes of the experimental $^2H$ solid-state nuclear magnetic resonance (SSNMR) spectra were best simulated by assuming the coexistence of a mosaic spread of bilayers containing pore structures and a fasttumbling isotropic phase or a hexagonal phase. Within a few days of incubation in a hydration chamber, an isotropic phase and a pore structure were induced by magainin 2, while in case of aurein 3.3 only an isotopic phase was induced in the presence of a bilayer phase. After an incubation period of over 100 days, alignment of the bilayers increased and the amount of the pore structure decreased in case of magainin 2. In contrast with magainin 2, aurein 3.3 induced a hexagonal phase at the peptide-to-lipid ratio of 1/20 and, interestingly, cholesterol was not found in the hexagonal phase induced by aurein 3.3. The experimental results indicate that magainin 2 is more effective in disrupting lipid bilayers containing cholesterol than aurein 3.3.

Antifungal Activities of Magainin-2 Hybrid Peptides against Trichosporon beigelii

  • LEE, DONG GUN;SONG YUB SHIN;SUNG GU LEE;KIL LYONG KIM;MYUNG KYU LEE;KYUNG SOO HAHM
    • Journal of Microbiology and Biotechnology
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    • 제7권1호
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    • pp.49-51
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    • 1997
  • In order to obtain a hybrid synthetic peptide with a more potent antifungal activity than magainin-2 but without hemolytic activity, four hybrid peptides were designed from the sequences of magainin 2 and cecropin A and their antifungal activities against Trichosporon beigelii were investigated. The result showed that analogue 2 and 4 exhibited better antifungal activity against T. beigelii than magainin-2 but no hemolytic activities. The peptides, therefore, could be used as models for the development of potent antifungal peptides.

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클로렐라 시스템에서 항균펩타이드 Magainin 2의 효율적인 세포외 분비 (Efficient Extracellular Secretion of the Antimicrobial Peptide Magainin 2 in the Chlorella-based System)

  • 정유정;황재윤;김성천
    • 한국해양바이오학회지
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    • 제16권1호
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    • pp.55-62
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    • 2024
  • Various antimicrobial peptides (AMPs) from microalgae have shown antibacterial, antiviral, antifungal, anticancer, and antioxidant effects, and play crucial roles in medical applications, aquaculture-related disease management, and the food industry. Magainin 2 (MAG2), an AMP, exhibits high antibacterial and antitumor activity, necessitating an efficient recombinant expression system for low-cost, large-scale production. To enhance MAG2 secretion efficiency in Chlorella, we constructed the SS:MAG2:His vector using the known Chlamydomonas reinhardtii CA1 signal sequence (SS) and obtained a stable transformant via an Agrobacterium-mediated transformation method and RT-qPCR. ELISA results revealed that the MAG2 content secreted into the medium by the SS:MAG2:His transformants increased proportionally with mRNA expression. These findings offer a strategy for high MAG2 secretion in the Chlorella vulgaris platform, potentially minimizing downstream processing costs.

Cecropin A-Magainin 2 유도체 펩티드의 Trichosporon beigelii에 대한 항진균 활성 및 인간 적혈구 세포에 대한 용혈활성 (Fungicidal and Hemolytic Activity of Cecropin A-Magainin 2 Analogue Peptides against Tri-chospoon beigelii and Human Red Blood Cells)

  • 이동건;신송엽;이명규;함경수
    • 미생물학회지
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    • 제33권3호
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    • pp.170-174
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    • 1997
  • 강한 항진균 활성을 나타내며, 낮은 적혈구 용혈활성을 갖는 새로운 합성 펩티드를 얻기 위하여 cecropin A(1-8)-magainin 2(1-12) 및 이들의 유사체들을 설계하고 이들을 고상법에 의하여 합성하였다. 합성 펩티드의 항진균 활성은 Trichosporon beigelii에 대한 성장억제능에 의하여 측정하였으며, 세포독성은 인간의 적혈구 세포에 대한 용혈활성에 의하여 측정하였다. 펩티드의 양쪽 친매성의 증가는 항진균활성보다는 적혈구 용혈황성에 큰 영향을 미쳤다. Cecropin A(1-8)-magainin 2(1-12)의 12번 아미노산이 Lys을 Ala으로 치환시킨 유사체 펩티드(A2)는 가장 강한 항진균활성(minimum inhibitory concentration : 2.5.$\mu$g/ml)을 나타내며 비교적 낮은 적혈구 용혈활성(200.$\mu$g/ml의 펩티드 농도에서 0.5% hemolysis를 나타냄)을 나타내었다. 따라서 A2의 펩티드는 세포독성을 갖지 않으며 강한 항진균 활성을 가지는 모델로서 유용하게 사용될 것이다.

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Structure-Antifungal Activity Relationships of Cecropin A-Magainin 2 and Cecropin A-Melittin Hybrid Peptides on Pathogenic Fungal Cells

  • Lee, Dong-Gun;Jin, Zhe-Zhu;Shin, Song-Yub;Kang, Joo-Hyun;Hahm, Kyung-Soo;Kim, Kil-Lyong
    • Journal of Microbiology and Biotechnology
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    • 제8권6호
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    • pp.595-600
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    • 1998
  • In order to investigate a relationship of the structure-antifungal and hemolytic activities between cecropin A(1-8)-magainin 2(1-12) and cecropin A(1-8)-melittin(1-12) hybrid peptides, several analogues with amino acid substitution at positions 10 (Ile) and 16 (Ser) were designed and synthesized. The increase of the hydrophobicity by substituting with Leu, Phe, and Trp at position 16 in cecropin A(1-8)-magainin 2(1-12) did not have a significant effect on antifungal activity but caused a remarkable increase in hemolytic activity. These results indicate that the hydrophobic property at position 16 of cecropin A(1-8)-magainin 2(1-12) is more correlated to hemolytic activity than to antifungal activity. Replacement with Pro at position 10 of cecropin A(1-8)- magainin 2(1-12) and cecropin A(1-8)-melittin (1-12) caused a remarkable decrease in a-helical contents in the 50% TFE solution and induced a reduction in lytic activity against Aspergillus flavus, and Aspergillus fumigatus. These results demonstrate that flexibility at the central hinge region is essential for lytic activity against fungal cells and $\alpha$-helicity of the peptides.

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Antifungal Activities of Peptides with the Sequence 10-17 of Magainin 2 at the N-termini against Aspergillus fumigatus (Antifungal activities of peptides with the sequence 10-17 of magainin 2 at the N-termini against aspergillus fumigatus)

  • Lee, Myung Kyu;Lee, Dong Gun;Shin Song Yub;Lee, Sung Gu;Kang Joo Hyun;Hahm, Kyung Soo
    • Journal of Microbiology
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    • 제34권3호
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    • pp.274-278
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    • 1996
  • Two peptides, MA-inv AND MA-ME, with the sequence 10-17 of maganin 2 at their-N-termini were designed and synthesized. The peptides had higher antifungal activities against Aspergilus fumigatus without hemolytic activities. The minimal inhibition concentratory (MIC) values of both peptides against A. fumigatus were 5 .mu.g/ml, whereas those of the native peptides, magainin 2 and melittin, were 10.mu.g/ml. At 3 .mu.g/ml, MA-inv and MA-ME inhibited the mycelium growth of A. fumigatus by 94.6% and 97.3% respectively, whereas magainin 2 and melittin inhibited by 62.2% and 32.4, respectively. MA-inv showed up to 80% inhibition of (1, 3)-.betha.-D-glucan synthase activity of A. fumigatus. The peptides also showed up to 80% inhibition of (1, 3)-.betha.-D glucan synthase activity of A. fumigatus. The peptides also showed antifungal activities for other fungi of Aspergillus sp. However, the antibiotic activities of MA-ME against Escherichia coli, Bacillus subtilis and Fusarium oxysporum were more effective than those of MA-inv, suggesting that the C-terminal sequences of MA-inv and MA-ME may also influence their antibiotic activities. These results suggest that the N-terminal sequence of the designed peptides, KKFGKAFV, is important for their antifungal activities against A. fumigatus and their C- terminal sequences are related to the organism selectivity.

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항균성 펩타이드인 magainin 2의 활성에 대한 고체 핵자기 공명 분광 연구 (A solid-state NMR study on the activity of an antimicrobial peptide, magainin 2)

  • 김철
    • 분석과학
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    • 제24권6호
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    • pp.460-466
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    • 2011
  • 얇은 유리판 위에 정렬된 지질 이중막에 작용하는 항균성 펩타이드 magainin 2의 작용활성을 고체 핵자기 공명 분광법을 이용하여 조사하였다. 수화에 따른 지질 이중막의 파괴정도를 파악하기 위해 두 가지 수화 상태에서 실험이 이루어졌다. 95%의 상대 습도에서 수화된 지질 이중막에서는 약 15% 정도의 지질 이중막이 파괴되었으며, 완전히 수화된 지질 이중막에서는 약 20% 정도의 지질 이중막이 파괴되었다. 두 가지 시료 제조방법에 따른 지질 이중막 파괴 정도의 비교를 통해, 항균성 펩타이드의 지질 이중막 결합과정이 지질 이중막 파괴에 중요한 변수임을 알 수 있었다.

Structure-antibiotic activity of cecropin A(1-8)-magainin 2(1-12), cecropin A(1-8)-melittin(1-12) hybrid peptides and their analogues studied by NMR spectroscopy

  • Donghoon Oh;Songyub Shin;Joohyun Kang;Hahm, Kyung-soo;Kim, Killyong;Kim, Yangmee
    • 한국생물물리학회:학술대회논문집
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    • 한국생물물리학회 1999년도 학술발표회 진행표 및 논문초록
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    • pp.32-32
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    • 1999
  • Cecropin A(1-8)-magainin 2(1-12) and cecropm A(1-8)-melittin(1-12) hybrid peptides were known to have potent antitumor and antibacterial activity. In particular, cecropm A(l-8)-magainin 2(1-12) has powerful antibacterial and antitumor activity with no hemolytic effect.(omitted)

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항균성 펩타이드에 의한 지질 이중막의 상 변화에 대한 NMR 연구 (An NMR Study on the Phase Changes of Lipid Bilayers by Antimicrobial Peptides)

  • 김철
    • 대한화학회지
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    • 제54권2호
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    • pp.183-191
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    • 2010
  • 1-Palmitoyl-$d_{31}$-2-oleoyl-sn-glycero-3-phosphatidylcholine (POPC_$d_{31}$)로 이루어진 지질 이중막에 항균성 펩타이드 magainin 2와 aurein 3.3이 작용했을 때 일어나는 상변화를 중수소 고체 핵자기 공명 스펙트럼을 관측하여 탐구하였다. 측정된 중수소 고체 핵자기 공명 스펙트럼의 선모양을 이론적 모델 구조를 통하여 모사함으로써, 펩타이드-지질 혼합상태의 기하학적 구조상수 및 동력학적 표면 확산 계수 등을 구하였다. 펩타이드의 혼합 이후 5일 이내의 짧은 작용시간에는 지질 이중막의 정렬이 파괴되는 현상이 나타났으나, 100일 이후에는 magainin 2에 의해서는 타원형 원환체 기공 (elliptic toroidal pore)이, aurein 3.3에 의해서는 6각형 단면 막대구조 상(hexagonal phase)이 관측되었다. 지질 이중막 표면의 전하밀도가 항균성 펩타이드의 작용에 미치는 효과를 보기 위해 산성 지질인 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylglycerol (POPG)를 함유한 POPC_$d_{31}$/POPG 지질 이중막에 대해서도 동일한 실험을 수행하였다. 동일한 ${\alpha}$-나선형 구조를 가지는 두 펩타이드가 두 종류의 지질 이중막에 작용하는 과정의 차이를 확인할 수 있었다.