In vitro cytotoxicity and antibiotic activity of polymyxin B nonapeptide

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In vitro cytotoxicity and antibiotic activity of polymyxin B nonapeptide.

Polymyxin B nonapeptide, prepared by enzymic removal of the fatty acyl diaminobutyric acid side chain from polymyxin B, was about 100-fold less toxic to K562 cells than polymyxin B. MICs of polymyxin B nonapeptide against a test panel of bacteria were 2- to 64-fold lower than those of polymyxin B.

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Effects of polymyxin B nonapeptide on Aeromonas salmonicida.

In contrast to polymyxin B-susceptible gram-negative bacteria of human origin, the fish pathogen Aeromonas salmonicida was resistant to sensitization by polymyxin B nonapeptide (PMBN) to hydrophobic antibiotics. Similarly, sensitization of A. salmonicida strains by PMBN to the bactericidal action of brook trout (Salvelinus fontinalis) serum complement was less pronounced than the similar effect...

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Antibacterial synergism of polymyxin B nonapeptide and hydrophobic antibiotics in experimental gram-negative infections in mice.

Polymyxin B nonapeptide, derived by cleavage of the fatty acyl diaminobutyric acid from polymyxin B, is considerably less toxic, lacks bactericidal activity, and retains its ability to render gram-negative bacteria susceptible to several antibiotics by permeabilizing their outer membranes. The peptide rendered all 53 polymyxin-susceptible strains tested more susceptible to novobiocin, lowering ...

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Effect of polymyxin B nonapeptide on daptomycin permeability and cell surface properties in Pseudomonas aeruginosa, Escherichia coli, and Pasteurella multocida.

The present study was carried out to determine if sensitization of Gram-negative bacteria to the polyanionic antibiotic daptomycin by cationic molecules can be explained on the basis of decreased cell surface charge in order to better understand intrinsic resistance. Turbidimetric assessments of batch cultural growth kinetics revealed the outer membrane permeabilizer polymyxin B nonapeptide sen...

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The antibiotic polymyxin B modulates P2X7 receptor function.

The natural peptide polymyxin B (PMB) is a well-known and potent antibiotic that binds and neutralizes bacterial endotoxin (LPS), thus preventing its noxious effects among LPS-mediated endotoxin shock in animal models. We have investigated the effect of PMB on responses mediated by the P2X(7)R in HEK293 and K562 cells transfected with P2X(7) cDNA and in mouse and human macrophages. In addition,...

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ژورنال

عنوان ژورنال: Antimicrobial Agents and Chemotherapy

سال: 1986

ISSN: 0066-4804,1098-6596

DOI: 10.1128/aac.30.2.340