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