Use of a real-time polymerase chain reaction thermocycler to study bacterial cell permeabilization by antimicrobial peptides.
Clarisse Bourbon, Claire Bry, Caroline Roggemans, Clelia Soulard, Céline Thizon, Bertrand Garbay
Index: Anal. Biochem. 381(2) , 279-81, (2008)
Full Text: HTML
Abstract
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.
Related Compounds
Related Articles:
2010-08-01
[Exp. Parasitol. 125(4) , 342-7, (2010)]
2012-02-01
[Peptides 33(2) , 197-205, (2012)]
Magainins as paradigm for the mode of action of pore forming polypeptides.
1998-11-10
[Biochim. Biophys. Acta 1376 , 391-400, (1998)]
1999-08-10
[Biochemistry 38 , 10377, (1999)]
A critical comparison of the hemolytic and fungicidal activities of cationic antimicrobial peptides.
1999-04-23
[FEBS Lett. 449 , 105, (1999)]