A new method to study permeation of β‐lactam antibiotics into reconstituted vesicles from the outer membrane of <i>Pseudomonas aeruginosa</i> NCTC 10662

Phospholipid bilayer permeability of fi-lactam antibiotics was determined using liposomes enclosing ,& lactamase. There was good correlation between the permeability and hydrophobicity within the analogous &lactams. However, the effect of hydrophobic character on the permeability parameter was very different between the groups. Moderately hydrophilic penicillins such as benzylpenicillin and ampicillin showed very high permeability compared with cephalosporins. Penicillins having hindered side chains such as oxacillin and methicillin showed moderate permeability taking into account their hydrophobicity. These observations are suggestive of outer membrane permeation of these fl-lactams via routes other than the porin pore, especially in porin-deficient mutants of gram-negative bacteria. B-LactamLipid-bilayer permeability Hydrophobicity Liposome Outer membrane fl-Lactamase

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The effect of hydrophobicity of β‐lactam antibiotics on their phospholipid bilayer permeability

Yamaguchi¹,

Hiruma²,

Sawai³

1983

FEBS Letters

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Final steps of the maturation of Omp F, a major protein from the outer membrane of Escherichia coli

1985

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Pulse-labelling experiments with E. coli cells allowed us to follow the incorporation of de novo proteins into the outer membrane of the cell envelope. Labelled membrane samples containing increasingly different levels of newly synthesized Omp F protein were subjected to chemical cross-linking with a bifunctional cleavable reagent in order to investigate the process of trimer formation of the protein. From the results obtained, we conclude that the formation of functional Omp F trimers is substantially delayed to, and can be distinguished from, the incorporation of Omp F monomers to the outer membrane. E. coli Outer membrane Porin protein Omp F Membrane biogenesis Chemical cross-linking

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Role of permeability barriers in resistance to β-lactam antibiotics

Nikaido

1985

Pharmacology & Therapeutics

127

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A new method to study permeation of β‐lactam antibiotics into reconstituted vesicles from the outer membrane of Pseudomonas aeruginosa NCTC 10662

Cited by 5 publications

References 16 publications

The effect of hydrophobicity of β‐lactam antibiotics on their phospholipid bilayer permeability

The effect of hydrophobicity of β‐lactam antibiotics on their phospholipid bilayer permeability

Final steps of the maturation of Omp F, a major protein from the outer membrane of Escherichia coli

Role of permeability barriers in resistance to β-lactam antibiotics

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