• Bulletin of the Korean Chemical Society
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• v.35 no.5
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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.

• Journal of Microbiology and Biotechnology
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• v.7 no.1
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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.

• Korean Journal of Microbiology
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• v.33 no.3
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• pp.170-174
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• 1997

In order to design a novel synthetic peptide with improved fungicidal activity but low hemolytic activity, a hybrid peptide, cecropin A(l-8)-magainin 2(1-12), and its analogue peptides were synthesized by the solid phase method. Antifungal and hemolytic activities of the synthetic peptides were assessed by the growth inhibition against Trichosporon beigelii and the cell membrane lysis against human red hlood cells, respectively. Analogue 2 in which Lys at position 12 in cecropin A(1-8)-magainin 2(1-12) was substituted with Ala showed most potent antifungal activity (MIC: 2.5.$\mu$g/ml) with minimal hemolytic activity (0.5% hemolysis at the (200.$\mu$g/ml peptide). This peptide (A2), therefore, could be useful as a model for further designing potent antifungal peptides without cytotoxicity.

• Journal of Microbiology and Biotechnology
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• v.8 no.6
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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.

• Journal of Microbiology
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• v.34 no.3
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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.

• Analytical Science and Technology
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• v.24 no.6
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• pp.460-466
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• 2011

The activity of an antimicrobial peptide, magainin 2, on lipid membranes was investigated using solid-state NMR and a new sampling method that employed mechanically aligned bilayers between thin glass plates. The experiments were performed at two hydration levels. At 95% hydration about 15% of the lipid bilayers were disrupted and at full hydration 20% were disrupted. From the comparison of two equilibrium states established by two sampling methods the importance of peptide binding to the lipid bilayer for whole membrane disruption was demonstrated.

• Proceedings of the Korean Biophysical Society Conference
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• 1999.06a
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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)

• Journal of the Korean Chemical Society
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• v.54 no.2
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• pp.183-191
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• 2010

The phase changes of 1-palmitoyl-$d_{31}$-2-oleoyl-sn-glycero-3-phosphatidylcholine (POPC_$d_{31}$) bilayers distorted by an antimicrobial peptide, a magainin 2 or an aurein 3.3 were investigated by using $^2H$ solid-state NMR (SSNMR) spectroscopy. From the theoretical simulation of the experimental $^2H$ solid-state NMR spectra the geometric structure constants and the lateral diffusion coefficients were obtained in the peptide-lipid mixture phases. Within five days of the peptide action on the lipid bilayers only the distorted alignment of the bilayers were measured but after 100 days an elliptic toroidal pore structure and an inverted hexagonal phase were formed in the presence of magainin 2 and aurein 3.3, respectively. In order to investigate the effect of an anionic lipid molecule on the actions of two peptides on the lipid bilayer, the same experiments were performed on the POPC_$d_{31}$/1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylglycerol (POPG) bilayer and the significant differences in the actions of two peptides on two bilayers of POPC_$d_{31}$ and POPC_$d_{31}$/POPG were measured.

• Proceedings of the Korean Magnetic Resonance Society Conference
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• 1999.06a
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• pp.29-29
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• 1999

• Journal of the Korean Magnetic Resonance Society
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• v.2 no.2
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• pp.120-130
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• 1998