Lactoferricin B causes depolarization of the cytoplasmic membrane of Escherichia coli ATCC 25922 and fusion of negatively charged liposomes

FEBS Lett. 2001 Mar 9;492(1-2):62-5. doi: 10.1016/s0014-5793(01)02233-5.

Abstract

Antimicrobial peptides have been extensively studied in order to elucidate their mode of action. Most of these peptides have been shown to exert a bactericidal effect on the cytoplasmic membrane of bacteria. Lactoferricin is an antimicrobial peptide with a net positive charge and an amphipatic structure. In this study we examine the effect of bovine lactoferricin (lactoferricin B; Lfcin B) on bacterial membranes. We show that Lfcin B neither lyses bacteria, nor causes a major leakage from liposomes. Lfcin B depolarizes the membrane of susceptible bacteria, and induces fusion of negatively charged liposomes. Hence, Lfcin B may have additional targets responsible for the antibacterial effect.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Cell Membrane / chemistry
  • Cell Membrane / drug effects*
  • Escherichia coli / drug effects*
  • Escherichia coli / metabolism
  • Escherichia coli / ultrastructure
  • Lactoferrin / analogs & derivatives*
  • Lactoferrin / pharmacology*
  • Liposomes / chemistry*
  • Liposomes / metabolism
  • Microbial Sensitivity Tests
  • Peptides

Substances

  • Anti-Bacterial Agents
  • Liposomes
  • Peptides
  • lactoferricin B
  • Lactoferrin