• Title/Summary/Keyword: Hemolytic activity

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Solution Conformation of an Antimicrobial Peptide Gaegurin 4

  • Suk, Jae-Eun;Baek, Hwa-Jin;Lee, Byeong-Jae;Han, Kyou-Hoon
    • 한국생물물리학회:학술대회논문집
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    • 한국생물물리학회 1997년도 학술발표회
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    • pp.13-13
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    • 1997
  • Gaegurin 4 is an antimicrobial peptide found in the skin of a Korean frog, Rana rugosa, known for its "wound-healing" effect for years. This 37-residue basic peptide binds to cell membranes and forms ion channels like other antimicrobial peptides but does not exhibit hemolytic activity.(omitted)

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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.

Hemolytic Activity of Culture Supernatant of Xenorhabdus nematophilus, a Symbiotic Bacterium of Entomopathogenic Nematodes

  • Ryu, Keun-Garp;Bae, Jun-Sung;Kwack, Kyu-Bum;Kwon, O-Yul;Park, Sun-Ho
    • Journal of Microbiology and Biotechnology
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    • 제12권3호
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    • pp.526-529
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    • 2002
  • Lysis of erythrocytes isolated from human, rabbit, and mouse blood samples was investigated with the culture supernatant of Xenorhabdus nematophilus in a primary form. Prior to use, the culture supernatant of the bacteria was concentrated and the concentrate was dialyzed against Tris-HCl buffer (10 mM, pH 8.1) by ultrafiltration using PM-5 membrane with a molecular weight cut-off of 5,000. At $30^{\circ}C$, the supernatant exhibited no lytic activity towards three types of erythrocytes. However, at $4^{\circ}C$, the supernatant showed selective lytic activity towards rabbit erythrocytes within 90 min. yet did not lyze human or mouse erythrocytes. Microscopic examination clearly revealed that most of the rabbit erythrocytes had been fumed into ghost forms.

식물의 렉틴 성분 스크리닝 (Screening of Plants for Lectins Constituents)

  • 정시련;정수민;이승호;전경희
    • 약학회지
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    • 제40권4호
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    • pp.387-393
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    • 1996
  • The erythrocytes agglutination test was applied to the common korean plants for lectin activity screening by using human blood. During the four years, 108 species from 46 families of floras were collected, identified and subjected to the test after being divided into several different parts. Only 13 species demonstrated strong lectin activities. Meanwhile 66 species did not shown any agglutination. All others were observed as having low activity or as having hemolytic constituents.

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Antitumor Components of Korean Basidiomycetes

  • Kim, Byong-Kak;Kim, Ji-Hyun;Kim, Ha-Won;Choi, Eung-Chil
    • 생약학회지
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    • 제17권1호
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    • pp.39-48
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    • 1986
  • To find antitumor components in the shake-cultured mycelia of Volvariella bombycina, the mycelia were extracted with hot water. After the extract was dialyzed and freeze-dried, a protein-polysaccharide fraction was obtained and examined for antitumor activity against the solid form of sarcoma 180 in ICR mice. It showed 60.3% inhibition ratio at a dose of 20mg/kg/day for 10 days. It was found to consist of a polysaccharide moiety and a protein moiety. After gel filtration on Sepharose 4B, Fraction B was obtained and showed the highest inhibition ratio of 71.1%. When the antitumor component was examined for immunopotentiating activity, it was found to increase the macrophage accumulation in the peritoneal cavity as well as the antibody production of the spleen cells of the mice.

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홑파래로부터 추출한 Rhamnan Sulfate의 항보체 활성 (Anticomplementary Activities of Rhamnan Sulfate extracted from Monostroma nitidum)

  • 빈재훈;김현대;류병호
    • 한국식품영양학회지
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    • 제9권4호
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    • pp.490-495
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    • 1996
  • 홑파래로부터 황산기를 함유한 다당체를 크로마토그래프로 분리정제하여 rhamnan sulfate가 항보체 활성화에 미치는 영향을 조사하였다. 항보체 활성능력은 F-4-3 획분을 비교군으로 Heparin H-180, Dextran과 비교해 결과 비교군보다 높았고, C4a와 C3a의 C convertase의 형성과 기능을 F-4-3 획분이 억제하였다. 이러한 보체 활성화 양식은 classical pathway 및 alternative pathway로도 경유함을 알 수 있었다.

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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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Interaction of Mastoparan B and Its Ala-Substituted Analogs with Phospholipid Bilayers

  • 박남규;서정길;구희정;김승호;Sannamu Lee;Gohsuke Sugihara;김광호;박장수;강신원
    • 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.

Gram-Positive Bacteria Specific Properties of Silybin Derived from Silybum marianum

  • Lee, Dong-Gun;Kim, Hyung-Keun;Park, Yoon-Kyung;Park, Seong-Cheol;Woo, Eun-Rhan;Jeong, Hye-Gwang;Hahm, Kyung-Soo
    • Archives of Pharmacal Research
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    • 제26권8호
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    • pp.597-600
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    • 2003
  • Silybin has a potent antibacterial activity, more potent than silymarin II, against gram-positive bacteria without hemolytic activity, whereas it has no antimicrobial activity against gram-negative bacteria or fungi. The mode of action of silybin against the gram-positive bacterial cell was examined by investigating the change in plasma membrane dynamics of bacterial cells using 1 ,6-diphenyl-1,3,5-hextriene (DPH) as a membrane probe and by assessing the inhibition of macromolecular synthesis using radiolabeled incorporation assay. The results showed that silybin inhibited RNA and protein synthesis on gram-positive bacteria.

Investigation of the Antifungal Activity and Mechanism of Action of LMWS-Chitosan

  • Park, Yoon-Kyung;Kim, Mi-Hyun;Park, Seong-Cheol;Cheong, Hyeon-Sook;Jang, Mi-Kyeong;Nah, Jae-Woon;Hahm, Kyung-Soo
    • Journal of Microbiology and Biotechnology
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    • 제18권10호
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    • pp.1729-1734
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    • 2008
  • Chitosan, a cationic polysaccharide, has been widely used as a dietary supplement and in a variety of pharmacological and biomedical applications. The antifungal activity and mechanism of action of low molecular weight water-soluble chitosan (LMWS-chitosan) were studied in fungal cells and vesicles containing various compositions of fungal lipids. LMWS-chitosan showed strong antifungal activity against various pathogenic yeasts and hyphae-forming fungi but no hemolytic activity or cytotoxicity against mammalian cells. The degree of calcein leakage was assessed on the basis of lipid composition (PC/CH; 10:1, w/w). Our result showing that LMWS-chitosan interacts with liposomes demonstrated that chitosan induces leakage from zwitterionic lipid vesicles. Confocal microscopy revealed that LMWS-chitosan was located in the plasma membrane. Finally, scanning electron microscopy revealed that LMWS-chitosan causes significant morphological changes on fungal surfaces. Its potent antibiotic activity suggests that LMWS-chitosan is an excellent candidate as a lead compound for the development of novel anti-infective agents.