• Journal of Microbiology and Biotechnology
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• 제9권3호
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• pp.276-281
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• 1999

In order to determine the functional region of the antifungal protein (AFP) isolated from Aspergillus giganteus responsible for growth inhibitory activity and the promotion of phospholipid vesicle aggregation, overlapping peptides covering the complete sequence of AFP were synthesized. The antibiotic activity against bacterial, fungal, and tumor cells, and the vesicle-aggregation activity of the synthetic peptides were investigated. The AFP functional sequence responsible for antibiotic and vesicle-aggregation activity was determined to be located within the region between AFP residues 19 to 32. AFP (19-32) exhibited an a-helical conformation in a cell membrane-like environment. AFP (19-32) displayed potent antibiotic activity against bacterial, fungal, and tumor cells without peptide toxicity as indicated by hemolysis. Accordingly, AFP (19-32) could be used as a good model for the design of effective antibiotic agents with powerful antibiotic activity yet without any cytotoxic effects against the host organism.

• Bulletin of the Korean Chemical Society
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• 제20권9호
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• pp.1078-1084
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• 1999

A synthetic cecropin A(1-13)-melittin(1-13) [CA-ME] hybrid peptide was known to be an antimicrobial peptide having strong antibacterial, antifungal and antitumor activity with minimal cytotoxic effect against human erythrocyte. Analogues were synthesized to investigate the influences of the flexible hinge region of CA-ME on the antibiotic activity. Antibiotic activity of the peptides was measured by the growth inhibition against bac-terial, fungal and tumor cells and vesicle-aggregating or disrupting activity. The deletion of Gln-Gly-Ile (P1) or Gly-Gln-Gly-Ile-Gly (P3) from CA-ME brought about a significant decrease on the antibiotic activities. In contrast, Gly-Ile-Gly deletion (P2) from CA-ME or Pro insertion (P5) instead of Gly-Gln-Gly-Ile-Gly of CA-ME retained antibiotic activity. This result indicated that the flexible hinge or β-bend structure provided by Gly-Gln-Gly-Ile-Gly, Gln-Gly, or Pro in the central region of the peptides is requisite for its effective antibiotic activity and may facilitate easily the hydrophobic C-terminal region of the peptide to penetrate the lipid bilayers of the target cell membrane. In contrast, P4 and P6 with Gly-Gln-Gly-Pro-Gly or Gly-Gln-Pro in the central region of the peptide caused a drastic reduction on the antibiotic activities. This result suggested that the con-secutive β-bend structure provided by Gly-Gln-Gly-Pro-Gly or Gly-Gln-Pro in the central hinge region of the peptide seems to interrupt the ion channel/pore formation on the target cell membranes.

• 한국연초학회지
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• 제17권2호
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• pp.103-108
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• 1995

Antibiotic and physico-chemical properties of an active compound from actinomycetes isolate G-37, of which the culture filtrate had an inhibitory effect against tobacco mosaic virus(W) infection, were examined. The active compound, which was purified by ethylacetate extraction, silica gel column chromatography, preparative thin layer chromatography, and high performance liquid chromatography, showed strong antibacterial activities especially against Gram-positive bacteria including Bacillus subtillis, Sarcina lutea and Staphylococcus aureus. From the IH-NMR, FAB/RfS, UV spectral data, and physicochemical properties, the active compound of G-37 appears to belong to a peptide antibiotic group. Among the known peptide antibiotics in the antibiotic group, No. 280, A-30912, and Taitomycin showed molecular weights and ultra violet spectrum similar to those of the active compound from G-37, but was not identical to the compound, which suggests that it may be a new peptide antibiotics.

• Journal of Microbiology and Biotechnology
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• 제15권5호
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• pp.1039-1046
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• 2005

The salt resistance of antibacterial activity and synergistic effect with clinically used antibiotic agents are critical factors in developing effective peptide antibiotic drugs. For this reason, we investigated the resistance of antibacterial activity to antagonism induced by NaCl and $MgCl_2$ and the synergistic effect of P20 with cefotaxime. P20 is a 20-residue synthetic peptide derived from a cecropin A (CA)-melittin(ME) hybrid peptide. In this study, P20 was found to have potent antibacterial activity against clinically isolated methicillin-resistant Staphylococcus aureus (MRSA) strains without hemolytic activity against human erythrocytes. The combination study revealed that P20 in combination with cefotaxime showed synergistic antibacterial activity in an energy-dependent manner. We also confirmed the synergism between P20 and cefotaxime by fluorescence-activated flow cytometric analysis by staining bacterial cells with propidium iodide (PI) and bis-(1,3-dibutylbarbituric acid) trimethine oxonol (BOX). This study suggests that P20 may be useful as a therapeutic antibiotic peptide with synergistic effect in combination with conventional antibiotic agents.

• BMB Reports
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• 제33권1호
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• pp.49-53
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• 2000

PMAP-23 is a 23-residue antimicrobial peptide derived from porcine myloid cells. In order to investigate the effects of two Pro residues at positions 12 and 15 of PMAP-23 on antibiotic activity, two analogues in which Ala was substituted for Pro residue at position 12 or 15 were synthesized. $Pro^{12}{\rightarrow}Ala$ (PMAPl) or $Pro^{15}{\rightarrow}Ala$(PMAP2) substitution in PMAP-23 caused a significant reduction on antitumor and phospholipid vesicle-disrupting activities, but did not cause a significant effect on antibacterial activity. PMAP-23 displayed the type I ${\beta}-turn$ structure with a negative ellipticity at near 205 om in SDS micelle, whereas PMAP1 and PMAP2 had a somewhat ${\alpha}-helical$ propensity in TFE solution, as compared to PMAP-23. These results suggest that two Pro residues of positions 12 and 15 in PMAP-23 play important roles in the formation of ${\beta}-turn$ structure on lipid membrane and its ${\beta}-turn$ structure may be essential for antibiotic activity including phospholipid vesicle-disrupting property.

• 공업화학
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• 제22권2호
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• pp.119-124
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• 2011

현재, 사람들은 많은 병에 노출되어 있다. 산업화의 빠른 변화는 생산시설의 자동화, 정보 통신 산업기술의 발달로 삶의 질이 향상되었으나, 신체활동의 감소와 환경오염으로 인해 환경적 스트레스와 병원균 감염 반응에 대한 인간의 면역체계가 악화되었다. 아울러 현재 약물의 오 남용으로 다재약물내성을 갖는 미생물들(multidrug-resistant microbes)과 암세포(tumor)의 출현으로 인해 새로운 항생제 개발이 시급하다. 그들 중 하나가 항생 펩타이드(antibiotic peptide)로 기존 약물과 비교하면 약물저항성이 거의 일어나지 않는다. 여러 가지 항생활성을 가지는 펩타이드들은 다양한 생명체로부터 동정되고 있다. 이 논문은 항생 펩타이드들의 활성과 적용분야에 대해 논하려 한다.

• Journal of Microbiology and Biotechnology
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• 제7권6호
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• pp.402-408
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• 1997

The antibiotic-producing strain HW-003 was screened from soil and found to be effective against the multidrug-resistant Staphylococcus aureus. The spore chain of HW-003 was retinaculiaperti, and the spore surface was spiny. Strain HW-003 has a LL-diaminopimelic acid isoform in the cell wall. The aerial mass color of the strain was gray, and the reverse side was yellow-brown. The strain produced melanin, but did not produce soluble pigments. According to the Taxon program, HW-003 showed best match with Streptomyces cyaneus. Antibiotic production reached a maximum after 72-h cultivation. The antibiotic was purified with silica gel column chromatography, octadecylsilyl column chromatography, and HPLC. The purified antibiotic, AMRSA1, showed strong inhibitory activity against multidrug-resistant Staphylococcus aureus and gram-positive bacteria. The molecular weight of AMRSA1 was about 1, 100. AMRSA1 was a peptide antibiotic containing alanine and serine.

• 한국미생물·생명공학회지
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• 제19권6호
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• pp.604-609
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• 1991

토양에서 분리한 Streptomyces nigrifaciens GMT-497호무터 G(+) bacteria에만 강한 항균활성을 갖는 항생물질 MT-497을 용매추출, silica column chromatography와 재결정화를 통하여 분리 정제하였다. MT-497의 UV, 융점, 원소분석, IR spectrum, $^1H-NMR$과 구성아미노산 분석을 통해 actinocin chromophore와 threonine, proline, methyl valine, sarcosine, aspartic acid로 구성된 peptide을 갖는 actinomvcin계열의 항생물질로 동정하였다.

• 한국미생물·생명공학회지
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• 제22권1호
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• pp.52-58
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• 1994

The induced antibiotic peptides were isolatde from the white-spotted folwer chafer, Protaetia brevitarsis by injection of E. coli suspension to the larvae of the insect. The antibacterial activity of the peptides were assayed by the plate growth ingibition method, and were purified by ion-exchange chromatography, reversed-phase HPLC, ion-exchange HPLC and SDS-PAGE etc. The peptides were estimated as 9 kDa in molecular weight and named Protaecin I and Protaecin II, respectively. Protaecin I and II have strong antibacterial activities against Gram-positivie and/or Gram-negative bacteria, and they are stable in the heat treatment and in the range of pH 2-12.

• 통합자연과학논문집
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• 제1권1호
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• pp.47-53
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• 2008

In a previous study, we showed that Cecropin A (1-8)-Magainin 2 (1-12) hybrid peptide (CA-MA)'s analogue, Anal P5, exhibit broad-spectrum antimicrobial activity. Anal P5, designed by flexible region (positions 9, 10)-substitution, Lys- (positions 4, 8, 14, 15) and Leu- (positions 5, 6, 12, 13, 16, 17, 20) substitutions, showed an enhanced antimicrobial and antitumor activity without hemolysis. The primary objective of the present study was to gain insight into the relevant mechanisms of antimicrobial activities of Anal P5 by using flow cytometric analysis. Anal P5 exhibits strong antifungal activity in a salt concentration independent manner. In addition, Anal P5 causes significant morphological alterations of the bacterial surfaces as shown by scanning electron microscopy, supporting its antibacterial activity. Its potent antibiotic activity suggests that Anal P5 is an excellent candidate as a lead compound for the development of novel antibiotic agents.