| Literature DB >> 23994526 |
Ho Jin Park1, Ki Mo Kang, Kevin Dybvig, Bok Luel Lee, Yong Woo Jung, In Hee Lee.
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 30 min 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.Entities:
Keywords: 1-palmytoyl-2-oleoyl l-α-phosphatidylcholine; 1-palmytoyl-2-oleoyl l-α-phosphatidylglycerol; AMP; Action mechanism; Antimicrobial peptide; CL; EPS; Liposome; Mycoplasma; NaP; PI; POPC; POPG; Phospholipid; SEM; SPM; TLC; Vsa; antimicrobial peptide; cardiolipin; exopolysaccharide; propidium iodine; scanning electron microscopy; sodium phosphate; sphingomyelin; two-dimensional thin layer chromatography; variable surface antigen
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Year: 2013 PMID： 23994526 DOI： 10.1016/j.febslet.2013.08.016
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124