1. Interaction of cationic antimicrobial peptides withMycoplasma pulmonis
- Author
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Ki Mo Kang, Kevin Dybvig, Bok Luel Lee, Yong Woo Jung, Ho Jin Park, and In Hee Lee
- Subjects
Biophysics ,Phospholipid ,medicine.disease_cause ,Biochemistry ,Mycoplasma pulmonis ,Microbiology ,chemistry.chemical_compound ,Mycoplasma ,Kanamycin ,Structural Biology ,Phosphatidylcholine ,Genetics ,medicine ,Lipid bilayer ,Molecular Biology ,POPC ,Phospholipids ,Liposome ,Cell Membrane ,Cell Biology ,Action mechanism ,chemistry ,Microscopy, Electron, Scanning ,Chromatography, Thin Layer ,Antimicrobial peptide ,Sphingomyelin ,Antimicrobial Cationic Peptides - Abstract
We investigated the mode of action underlying the anti-mycoplasma activity of cationic antimicrobial peptides (AMPs) using four known AMPs and Mycoplasma pulmonis as a model mycoplasma. Scanning electron microscopy revealed that the integrity of the M. pulmonis membrane was significantly damaged within 30min of AMPs exposure, which was confirmed by measuring the uptake of propidium iodine into the mycoplasma cells. The anti-mycoplasma activity of AMPs was found to depend on the binding affinity for phosphatidylcholine, which was incorporated into the mycoplasma membrane from the growth medium and preferentially distributed in the outer leaflet of the lipid bilayer.
- Published
- 2013
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