Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?

Nat Rev Microbiol. 2005 Mar;3(3):238-50. doi: 10.1038/nrmicro1098.


Antimicrobial peptides are an abundant and diverse group of molecules that are produced by many tissues and cell types in a variety of invertebrate, plant and animal species. Their amino acid composition, amphipathicity, cationic charge and size allow them to attach to and insert into membrane bilayers to form pores by 'barrel-stave', 'carpet' or 'toroidal-pore' mechanisms. Although these models are helpful for defining mechanisms of antimicrobial peptide activity, their relevance to how peptides damage and kill microorganisms still need to be clarified. Recently, there has been speculation that transmembrane pore formation is not the only mechanism of microbial killing. In fact several observations suggest that translocated peptides can alter cytoplasmic membrane septum formation, inhibit cell-wall synthesis, inhibit nucleic-acid synthesis, inhibit protein synthesis or inhibit enzymatic activity. In this review the different models of antimicrobial-peptide-induced pore formation and cell killing are presented.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Anti-Bacterial Agents / metabolism
  • Anti-Bacterial Agents / pharmacology*
  • Antimicrobial Cationic Peptides / pharmacology*
  • Antimicrobial Cationic Peptides / physiology
  • Bacteria / drug effects*
  • Bacterial Physiological Phenomena
  • Cell Membrane / drug effects
  • Drug Design
  • Drug Resistance, Bacterial / physiology
  • Humans
  • Permeability
  • Protein Conformation


  • Anti-Bacterial Agents
  • Antimicrobial Cationic Peptides