Use of a real-time polymerase chain reaction thermocycler to study bacterial cell permeabilization by antimicrobial peptides.
Antimicrobial peptides are good leads to develop new antibiotics, but knowledge of their mode of action is a prerequisite. Destruction of the microbial membranes through a detergent-like mechanism is one of these modes of action. This is usually studied by using a fluorescent nucleic acid stain such as SYTOX Green, which is impermeable to living cells. Using a simple protocol based on the use of a standard real-time thermocycler, we confirmed that the actions of the antimicrobial peptides LL-37 and magainin 2 on bacterial cells are different.
Bourbon
Clarisse
C
Ecole Supérieure de Technologie des Biomolécules de Bordeaux, Université Victor Segalen Bordeaux 2, 33076 Bordeaux Cedex, France.
Bry
Claire
C
Roggemans
Caroline
C
Soulard
Clelia
C
Thizon
Céline
C
Garbay
Bertrand
B
D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides / Q000378:metabolism / Q000494:pharmacology*; D054804:Cathelicidins; D002463:Cell Membrane Permeability / Q000187:drug effects*; D005456:Fluorescent Dyes / Q000737:chemistry; D054806:Magainins; D009930:Organic Chemicals / Q000737:chemistry; D016133:Polymerase Chain Reaction; D029867:Xenopus Proteins / Q000494:pharmacology
D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D054804:Cathelicidins; D005456:Fluorescent Dyes; D054806:Magainins; D009930:Organic Chemicals; C402795:SYTOX Green; D029867:Xenopus Proteins; C053301:magainin 2 peptide, Xenopus