J Bacteriol Virol.  2014 Jun;44(2):140-151. 10.4167/jbv.2014.44.2.140.

Mechanism of Action of Antimicrobial Peptides Against Bacterial Membrane

Affiliations
  • 1Research Center for Proteinaceous Materials (RCPM), Chosun University, Gwangju, Korea. y_k_park@chosun.ac.kr
  • 2Department of Biotechnology, Chosun University, Gwangju, Korea.

Abstract

Resistance to antibiotics is becoming a very serious problem, with so-called superbugs exhibiting resistance to nearly all conventional antibiotic drugs. Consequently, these organisms often cause severe illness and even death. Alternatives to conventional antibiotics are antimicrobial peptides (AMPs). These widely expressed short peptides, which have been isolated from insects, plants, marine organisms and mammals, including humans, show strong antimicrobial activity against both Gram-negative and Gram-positive bacteria. Most AMPs act by disrupting the bacterial membrane through "Barrel-stave", "Toroidal pore", "carpet" mechanism. In addition, AMPs may prevent septic shock through strongly binding lipopolysaccharides and lipoteichoic acid located on the bacterial membrane. The action mechanisms of AMP to minimize the likelihood developing resistance to the peptides would be particular advantage. For these reasons, we anticipate that AMPs will replace conventional antibiotic drugs in a variety of contexts.

Keyword

Superbug; Antimicrobial peptide; Lipopolysaccharides; Lipoteichoic acid; AMP mechanism

MeSH Terms

Anti-Bacterial Agents
Aquatic Organisms
Gram-Positive Bacteria
Humans
Insects
Lipopolysaccharides
Mammals
Membranes*
Peptides*
Shock, Septic
Anti-Bacterial Agents
Lipopolysaccharides
Peptides

Figure

  • Figure 1. Action mechanism of antimicrobial peptides (AMPs) on the bacterial membrane.

  • Figure 2. Binding affinity of antimicrobial peptide on the lipopolysaccharides (LPS) and lipoteichoic acid (LTA) in membranes of Gram negative and Gram-positive bacteria.


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