Permeation of bacterial cells, permeation of cytoplasmic and artificial membrane vesicles, and channel formation on lipid bilayers by peptide antibiotic AS-48

J Bacteriol. 1991 Jan;173(2):886-92. doi: 10.1128/jb.173.2.886-892.1991.

Abstract

Peptide AS-48 induces ion permeation, which is accompanied by the collapse of the cytoplasmic membrane potential, in sensitive bacteria. Active transport by cytoplasmic membrane vesicles is also impaired by AS-48. At low concentrations, this peptide also causes permeability of liposomes to low-molecular-weight compounds without a requirement for a membrane potential. Higher antibiotic concentrations induce severe disorganization, which is visualized under electron microscopy as aggregation and formation of multilamellar structures. Electrical measurements suggest that AS-48 can form channels in lipid bilayers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents* / pharmacology*
  • Bacterial Proteins*
  • Biological Transport / drug effects
  • Cell Membrane / drug effects
  • Cell Membrane / physiology
  • Cell Membrane Permeability / drug effects
  • Cytoplasm / drug effects
  • Cytoplasm / physiology
  • Enterococcus faecalis / drug effects
  • Enterococcus faecalis / physiology*
  • Freezing
  • Ion Channels / physiology*
  • Kinetics
  • Lipid Bilayers*
  • Membrane Potentials / drug effects
  • Models, Biological
  • Peptides / chemistry
  • Peptides / pharmacology
  • Phosphatidylcholines
  • Phospholipids
  • Rubidium / metabolism

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Ion Channels
  • Lipid Bilayers
  • Peptides
  • Phosphatidylcholines
  • Phospholipids
  • BacA protein, Enterococcus faecalis
  • asolectin
  • Rubidium