• 제목/요약/키워드: Antibacterial peptides

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Antibacterial Activity and Synergism of the Hybrid Antimicrobial Peptide, CAMA-syn

  • Jeong, Ki-Woong;Shin, So-Young;Kim, Jin-Kyoung;Kim, Yang-Mee
    • Bulletin of the Korean Chemical Society
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    • 제30권8호
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    • pp.1839-1844
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    • 2009
  • A 20-residue hybrid peptide CA(1-8)-MA(1-12) (CAMA) incorporating residues 1-8 of cecropin A (CA) and residues 1-12 of magainin 2 (MA) has high antimicrobial activity without toxicity. To investigate the effects of the total positive charges of CAMA on the antibacterial activity and toxicity, a hybrid peptide analogue (CAMA-syn) was designed with substitutions of $Ile^{10}\;and\;Ser^{16}$ with Lys. According to CD spectra, structure of CAMA-syn with increase of cationicity was very similar to that of CAMA in DPC micelle. CAMA-syn showed antimicrobial activity similar with CAMA while CAMA-syn has no hemolytic activity and much lower cytotoxicity against RAW 264.7 macrophage cells than CAMA. Also, CAMA and CAMA-syn significantly inhibited NO production by LPSstimulated RAW264.7 macrophage at 10.0∼20.0 $\mu$M. CAMA-syn displayed salt resistance on antimicrobial activity against Escherichia coli at the physiological concentrations of $CaCl_2\;and\;MgCl_2$. The combination studies of peptides and antibiotics showed that CAMA-syn has synergistic effects with synthetic compound and flavonoid against Enterococcus faecalis and VREF. CAMA-syn can be a good candidate for the development of new antibiotics with potent antibacterial and synergistic activity but without cytotoxicity.

Anti-adherence of Antibacterial Peptides and Oligosaccharides and Promotion of Growth and Disease Resistance in Tilapia

  • Peng, K.S.;She, R.P.;Yang, Y.R.;Zhou, X.M.;Liu, W.;Wu, J.;Bao, H.H.;Liu, T.L.
    • Asian-Australasian Journal of Animal Sciences
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    • 제20권4호
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    • pp.569-576
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    • 2007
  • Four hundred and fifty tilapias ($6.77{\pm}0.23$ g) were assigned randomly to six groups to evaluate the feasibility of the tested antibacterial peptides (ABPs) and oligosaccharides as substitutes for antibiotics. The control group was fed with a commercial tilapia diet; other five groups were fed with the same commercial diet supplemented with konjac glucomannan (KGLM), cluster bean galactomannan (CBGAM), and three animal intestinal ABPs derived from chicken, pig and rabbit at 100 mg/kg respectively. After 21 days of feeding, growth, disease resistance, and in vivo anti-adherence were determined. Furthermore, the inhibitory effect of tested agents on adhesion of Aeromonas veronii biovar sobria (A.vbs) strain BJCP-5 to tilapia enteric epithelia in vitro was assessed by cell-ELISA system. As a result, the tested agents supplemented at 100 mg/kg show significant benefit to tilapia growth and disease resistance (p<0.05), and the benefit may be correlated with their interfering in the contact of bacteria with host mucosal surface. Although none of the tested agents did inhibit the growth of BJCP-5 in tryptic soy broth at $100{\mu}g/ml$, all of them did inhibit the adhesion of A.vbs to tilapia enteric epithelia in vivo and in vitro. In vitro mimic assays show that three ABPs at low concentrations of $25{\mu}g/ml$ and $2.5{\mu}g/ml$ have the reciprocal dose-dependent anti-adherence effect. The inhibition of ABPs may be correlated with a cation bridging and/or receptor-ligand binding, but not with hydrophobicity. The KGLM and CBGAM inhibited the adherence of BJCP-5 to tilapia enteric epithelia with dose-dependent manner in vitro, and this may be through altering bacterial hydrophobicity and interfering with receptor-ligand binding. Our results indicate that the anti-adherence of the tested ABPs and oligosaccharides may be one of the mechanisms in promoting tilapia growth and resistance to A.vbs.

호박벌 유래 디펜신 유전자의 분자적 특성분석 및 항균 활성 (Antimicrobial activity and characterization for defensin of synthetic oligopeptides derived from Bombus ignitus)

  • 강희윤;김인우;이준하;권용남;윤은영;윤형주;김성렬;김익수;황재삼
    • 한국잠사곤충학회지
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    • 제50권2호
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    • pp.161-165
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    • 2012
  • 호박벌 유래 디펜신의 전체 아미노산 서열의 구조 분석 후에 항균활성을 갖는 서열을 선발하였고, 전체 및 펩타이드 길이와 구조적 차이에 대한 종합적인 결과로서 기존에 보고되어진 ${\alpha}$-helix 구조의 펩타이드 보다는 ${\beta}$-sheet의 일부 서열과 ${\alpha}$-helix의 서열이 공존할 때 항균 활성이 보다 뛰어남을 확인하였다. 특히 시스테인-아르기닌 (38C-39R)이 포함되어 있는 펩타이드 서열에서 항균력이 우수하였고, 이는 세포벽에 친화력이 있는 염기성 펩타이드의 특성으로 예상하고 있다.

닭과 돼지의 항균펩타이드 NK-Lysin으로부터 조합된 펩타이드의 In Vitro 항균효과 (In Vitro Antibacterial Effects of the Chimeric Peptides from Chicken and Pig Antimicrobial Peptide NK-Lysin)

  • 홍여진;이기용;양수진;현순 릴레호이;홍영호
    • 한국가금학회지
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    • 제49권2호
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    • pp.69-77
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    • 2022
  • 가축에서 항생제의 남용은 항생제 내성균의 발생을 유도하므로 가축과 사람의 건강을 위협할 수 있다. 이에 따라 항생제를 대체할 수 있는 물질 중 하나로 항균펩타이드(antimicrobial peptides)가 연구되고 있다. 항균펩타이드는 12-50개의 아미노산으로 구성된 펩타이드로 숙주에 감염된 다양한 박테리아를 사멸시키고 면역작용을 조절하는 등 선천성 면역에 중요한 물질이다. 본 연구에서는 닭과 돼지의 NK-2를 조합하여 cpNK라는 chimeric 펩타이드를 합성하였으며 이것의 항균효과를 검증하였다. 그 결과, cpNK는 그람음성균인 E. coli와 Salmonella spp. 그리고 그람 양성균인 L. monocytogenes과 S. aureus를 사멸시켰으며, cpNK는 그람음성균에서 더 강력한 살균효과를 보였다. 특히, cpNK는 메티실린 내성 황색포도상구균 (methicillin-resistant Staphylococcus aureus, MRSA)에 대해서도 항균효과를 보여주었다. 또한, 27aa인 cpNK의 크기를 줄인 21aa의 cpNK-a1과 13aa의 cpNK-a2를 합성하여 마찬가지로 항균효과를 측정한 결과, cpNK보다는 약한 항균효과를 보였지만 여러 병원균의 생존율을 감소시켰다. 따라서 본 연구를 통해 우수한 항균효과를 갖는 cpNK와 cpNK로부터 유도된 펩타이드들을 항생제 대체제로 사용할 수 있는 가능성을 확인할 수 있었다.

RV-23, a Melittin-Related Peptide with Cell-Selective Antibacterial Activity and High Hemocompatibility

  • Zhang, Shi-Kun;Ma, Qian;Li, Su-Bo;Gao, Hong-Wei;Tan, Ying-Xia;Gong, Feng;Ji, Shou-Ping
    • Journal of Microbiology and Biotechnology
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    • 제26권6호
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    • pp.1046-1056
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    • 2016
  • RV-23 is a melittin-related antibacterial peptide (MRP) with lower cytotoxicity than either melittin or AR-23, another MRP. The aim of this study was to explore the mechanism of RV-23's antibacterial selectivity and its hemocompatibility. The results showed that all the peptides exhibited lytic activity against Staphylococcus aureus and Escherichia coli, with RV-23 showing the highest potency. Moreover, RV-23 had lower cytotoxicity than melittin or AR-23 at their minimal inhibitory concentration. In addition, CD experiments showed that melittin, RV-23, and AR-23 all had a typical α-helical structure, and RV-23 had the lowest α-helix content. The structural information showed that RV-23 has the lowest hydrophobicity and highest hydrophobic moment. Because hydrophobicity and α-helix content are believed to correlate with hemolysis, the results indicate that the selective lytic activity against bacteria of RV-23 may be due to its low hydrophobicity and α-helicity, which lead to low cytotoxicity without affecting antibacterial activity. Furthermore, RV-23 did not affect the structure and function of blood components such as red blood cells, platelets, albumin, and the blood coagulation system. In conclusion, RV-23 is a cell-selective antibacterial peptide with high hemocompatibility due to its unique structure.

Synthesis and Biological Characterization of Indolicidin Analogues

  • Lim, Yong-Beom;Pyun, Jae-Chul;Park, Jong-Sang
    • BMB Reports
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    • 제30권3호
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    • pp.229-233
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    • 1997
  • Indolicidin has been known to have a broad spectrum of antimicrobial activities against Gram negative and positive bacteria. Its eight analogues were chemically synthesized. The analogue design was based on the analysis of sequence to elucidate the role of some residues in the antibacterial mechanism of indolicidin. Bactericidal activities were assayed against Escherichia coli and Proteus vulgaris, and the membrane perturbing abilities of the peptides were assayed using a dye containing liposome. Among the eight analogues, $[Gly^4, Gly^6]-Indo,\;[Ile^6,Ile^8]-Indo,\;[Lys^{12}]-Indo$ and $[Thr^2,Tyr^9]-Indo$ showed enhanced antibacterial activities. These results suggest that proline and cationic residues are important in the bactericidal activity of indolicidin. We tried to describe the antimicrobial mechanism of indolicidin with these results.

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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.

Structural Studies of Porcine Myeloid Antibacterial Peptide, PMAP-23 in DPC micelles by NMR Spectroscopy

  • Park, Kyoungsoo;Songyub Shin;Kyungsoo Hahm;Kim, Yangmee
    • 한국생물물리학회:학술대회논문집
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    • 한국생물물리학회 2001년도 학술 발표회 진행표 및 논문초록
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    • pp.29-29
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    • 2001
  • Leukocytes are important elements in the host defense against microbial infections. A variety of antimicrobial peptides named as the cathelicidin family have been identified from leukocytes. PMAP-23 derived from porcine myeloid cells is an antimicrobial peptide belong to the cathelicidin family. PMAP-23 was reported to have potent growth inhibition activity against bacterial and tumor cells with no hemolytic activity.(omitted)

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Effect of a Bombyx mori Protein Disulfide Isomerase on Production of Recombinant Antibacterial Peptides

  • Goo, Tae-Won;Kim, Seong-Wan;Choi, Kwang-Ho;Kim, Seong-Ryul;Kang, Seok-Woo;Park, Seung-Won;Yun, Eun-Young
    • International Journal of Industrial Entomology and Biomaterials
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    • 제26권2호
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    • pp.119-123
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    • 2013
  • The insect baculovirus expression vector system (BEVS) is useful for producing biologically active recombinant proteins. However, the overexpression of heterologous proteins using this system often results in misfolded proteins and the formation of protein aggregates. To overcome this limitation, we developed a versatile baculovirus expression and secretion system using Bombyx mori protein disulfide isomerase (bPDI) as a fusion partner. bPDI gene fusion was found to improve the secretions and antibacterial activities of recombinant nuecin and enbocin proteins. Thus, we conclude that bPDI gene fusion is a useful addition to BEVS for the large-scale production of bioactive recombinant proteins.

Antibacterial Activity of Recombinant Pig Intestinal Parasite Cecropin P4 Peptide Secreted from Pichia pastoris

  • Song, Ki-Duk;Lee, Woon-Kyu
    • Asian-Australasian Journal of Animal Sciences
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    • 제27권2호
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    • pp.278-283
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    • 2014
  • Cecropins (Cec) are antibacterial peptides and their expression is induced in a pig intestinal parasite Ascaris suum by bacterial infection. To explore the usefulness of its activity as an antibiotic, CecP4 cDNA was prepared and cloned into the pPICZ B expression vector and followed by the integration into AOX1 locus in Pichia pastoris. The supernatants from cell culture were collected after methanol induction and concentrated for the test of antimicrobial activity. The recombinant P. patoris having CecP4 showed antimicrobial activity when tested against Staphyllococcus aureus in disc diffusion assay. We selected one of the CecP4 clones (CecP4-2) and performed further studies with it. The growth of recombinant P. pastoris was optimized using various concentration of methanol, and it was found that 2% methanol in the culture induced more antibacterial activity, compared to 1% methanol. We extended the test of antimicrobial activity by applying the concentrated supernatant of CecP4 culture to Pseudomonas aeruginosa and E. coli respectively. Recombinant CecP4 also showed antimicrobial activity against both Pseudomona and E. coli, suggesting the broad spectrum of its antimicrobial activity. After improvements for the scale-up, it will be feasible to use recombinant CecP4 for supplementation to the feed to control microbial infections in young animals, such as piglets.