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  • American Society for Microbiology  (3)
  • 1995-1999  (3)
  • Medicine  (3)
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  • American Society for Microbiology  (3)
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  • 1995-1999  (3)
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  • Medicine  (3)
RVK
  • 1
    Online Resource
    Online Resource
    Salt-Resistant Alpha-Helical Cationic Antimicrobial Peptides
    American Society for Microbiology ; 1999
    In:  Antimicrobial Agents and Chemotherapy Vol. 43, No. 7 ( 1999-07), p. 1542-1548
    Details
    In: Antimicrobial Agents and Chemotherapy, American Society for Microbiology, Vol. 43, No. 7 ( 1999-07), p. 1542-1548
    Abstract: Analogues based on the insect cecropin–bee melittin hybrid peptide (CEME) were studied and analyzed for activity and salt resistance. The new variants were designed to have an increase in amphipathic α-helical content (CP29 and CP26) and in overall positive charge (CP26). The α-helicity of these peptides was demonstrated by circular dichroism spectroscopy in the presence of liposomes. CP29 was shown to have activity against gram-negative bacteria that was similar to or better than those of the parent peptides, and CP26 had similar activity. CP29 had cytoplasmic membrane permeabilization activity, as assessed by the unmasking of cytoplasmic β-galactosidase, similar to that of CEME and its more positively charged derivative named CEMA, whereas CP26 was substantially less effective. The activity of the peptides was not greatly attenuated by an uncoupler of membrane potential, carbonyl cyanide- m -chlorophenylhydrazone. The tryptophan residue in position 2 was shown to be necessary for interaction with cell membranes, as demonstrated by a complete lack of activity in the peptide CP208. Peptides CP29, CEME, and CEMA were resistant to antagonism by 0.1 to 0.3 M NaCl; however, CP26 was resistant to antagonism only by up to 160 mM NaCl. The peptides were generally more antagonized by 3 and 5 mM Mg 2+ and by the polyanion alginate. It appeared that the positively charged C terminus in CP26 altered its ability to permeabilize the cytoplasmic membrane of Escherichia coli , although CP26 maintained its ability to kill gram-negative bacteria. These peptides are potential candidates for future therapeutic drugs.
    Type of Medium: Online Resource
    ISSN: 0066-4804 , 1098-6596
    URL: Article
    DOI: 10.1128/AAC.43.7.1542
    RVK:
    XA 24552
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1999
    detail.hit.zdb_id: 1496156-8
    SSG: 12
    SSG: 15,3
    Location Call Number Limitation Availability
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    Online Resource
  • 2
    Online Resource
    Online Resource
    Biological Properties of Structurally Related α-Helical Cationic Antimicrobial Peptides
    American Society for Microbiology ; 1999
    In:  Infection and Immunity Vol. 67, No. 4 ( 1999-04), p. 2005-2009
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 67, No. 4 ( 1999-04), p. 2005-2009
    Abstract: A series of α-helical cationic antimicrobial peptide variants with small amino acid changes was designed. Alterations in the charge, hydrophobicity, or length of the variant peptides did not improve the antimicrobial activity, and there was no statistically significant correlation between any of these factors and the MIC for Pseudomonas aeruginosa , Escherichia coli , or Salmonella typhimurium . Individual peptides demonstrated synergy with conventional antibiotics against antibiotic-resistant strains of P. aeruginosa . The peptides varied considerably in the ability to bind E. coli O111:B4 lipopolysaccharide (LPS), and this correlated significantly with their antimicrobial activity and ability to block LPS-stimulated tumor necrosis factor and interleukin-6 production. In general, the peptides studied here demonstrated a broad range of activities, including antimicrobial, antiendotoxin, and enhancer activities.
    Type of Medium: Online Resource
    ISSN: 0019-9567 , 1098-5522
    URL: Article
    DOI: 10.1128/IAI.67.4.2005-2009.1999
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1999
    detail.hit.zdb_id: 1483247-1
    Location Call Number Limitation Availability
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    Online Resource
  • 3
    Online Resource
    Online Resource
    Biological Properties of Structurally Related α-Helical Cationic Antimicrobial Peptides
    American Society for Microbiology ; 1999
    In:  Infection and Immunity Vol. 67, No. 4 ( 1999), p. 2005-2009
    Details
    In: Infection and Immunity, American Society for Microbiology, Vol. 67, No. 4 ( 1999), p. 2005-2009
    Type of Medium: Online Resource
    ISSN: 1098-5522 , 0019-9567
    URL: Article
    DOI: 10.1128/.67.4.2005-2009.1999
    RVK:
    XA 10000
    Language: English
    Publisher: American Society for Microbiology
    Publication Date: 1999
    detail.hit.zdb_id: 1483247-1
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
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