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The interactions of histidine-containing amphipathic helical peptide antibiotics with lipid bilayers. The effects of charges and pH

Vogt, T C ; Bechinger, B

The Journal of biological chemistry, 1999-10, Vol.274 (41), p.29115-29121 [Periódico revisado por pares]

United States

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  • Título:
    The interactions of histidine-containing amphipathic helical peptide antibiotics with lipid bilayers. The effects of charges and pH
  • Autor: Vogt, T C ; Bechinger, B
  • Assuntos: Amino Acid Sequence ; Anti-Bacterial Agents - chemistry ; Antimicrobial Cationic Peptides ; Bacillus subtilis ; Circular Dichroism ; Dextrans ; Escherichia coli ; Fluorescein-5-isothiocyanate - analogs & derivatives ; Fluoresceins ; Fluorescent Dyes ; Histidine - chemistry ; Hydrogen-Ion Concentration ; Lipid Bilayers - chemistry ; Liposomes - chemistry ; Molecular Sequence Data ; peptide antibiotics ; Peptides ; Protein Structure, Secondary ; Spectrometry, Fluorescence
  • É parte de: The Journal of biological chemistry, 1999-10, Vol.274 (41), p.29115-29121
  • Notas: ObjectType-Article-2
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  • Descrição: The alpha-helix of the designed amphipathic peptide antibiotic LAH(4 )(KKALLALALHHLAHLALHLALALKKA-NH(2)) strongly interacts with phospholipid membranes. The peptide is oriented parallel to the membrane surface under acidic conditions, but transmembrane at physiological pH (Bechinger, B. (1996) J. Mol. Biol. 263, 768-775). LAH(4) exhibits antibiotic activities against Escherichia coli and Bacillus subtilis; the peptide does not, however, lyse human red blood cells at bacteriocidal concentrations. The antibiotic activities of LAH(4) are 2 orders of magnitude more pronounced at pH 5 when compared with pH 7.5. Although peptide association at low pH is reduced when compared with pH 7.5, the release of the fluorophore calcein from large unilamellar 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine or 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol vesicles is more pronounced at pH values where LAH(4) adopts an orientation along the membrane surface. The calcein release experiments thereby parallel the results obtained in antibiotic assays. Despite a much higher degree of association, calcein release activity of LAH(4) is significantly decreased for negatively charged membranes. Pronounced differences in the interactions of LAH(4) with 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol or 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine membranes also become apparent when the mechanisms of dye release are investigated. The results presented in this paper support models in which antibiotic activity is caused by detergent-like membrane destabilization, rather than pore formation by helical peptides in transmembrane alignments.
  • Editor: United States
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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