Interactions of an anionic antimicrobial peptide with Staphylococcus aureus membranes |
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Authors: | Dennison Sarah R Howe Jörg Morton Leslie H G Brandenburg Klaus Harris Frederick Phoenix David A |
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Institution: | a Faculty of Science, University of Central Lancashire, Preston PR1 2HE, UK b Forschungszentrum Borstel, Leibniz-Center for Medicine and Biosciences, Parkallee 10, D-23845 Borstel, Germany c Department of Forensic and Investigative Science, University of Central Lancashire, Preston PR1 2HE, UK |
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Abstract: | The antimicrobial activity of the anionic peptide, AP1 (GEQGALAQFGEWL), was investigated. AP1 was found to kill Staphylococcus aureus with an MLC of 3 mM and to induce maximal surface pressure changes of 3.8 mN m−1 over 1200 s in monolayers formed from lipid extract of S. aureus membranes. FTIR spectroscopy showed the peptide to be α-helical (100%) in the presence of vesicles formed from this lipid extract and to induce increases in their fluidity (Δν circa 0.5 cm−1). These combined data show that AP1 is able to function as an α-helical antimicrobial peptide against Gram-positive bacteria and suggest that the killing mechanism used by the peptide involves interactions with the membrane lipid headgroup region. Moreover, this killing mechanism differs strongly from that previously reported for AP1 against Gram-negative bacteria, indicating the importance of considering the effects of membrane lipid composition when investigating the structure/function relationships of antimicrobial peptides. |
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Keywords: | Anionic α-helical peptide Antimicrobial Staphylococcus aureus membrane Lipid extract Monolayer Langmuir-Blodgett Fourier transform infrared spectroscopy |
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