A31P NMR study of the interaction of amphibian antimicrobial peptides with the membranes of live bacteria |
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| Authors: | B C S Chia Y -H Lam M Dyall-Smith F Separovic and J H Bowie |
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| Institution: | (1) Department of Chemistry, University of Adelaide, SA 5005, Australia;(2) School of Chemistry, University of Melbourne, VIC 3010, Australia;(3) Department of Microbiology, University of Melbourne, VIC 3010, Australia;(4) School of Chemistry, University of Melbourne, VIC 3010, Australia |
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| Abstract: | Amphibian skin is a rich source of peptides that are specificto pathogens and act by disrupting bacterial membranes. Threeantimicrobial peptides were isolated from the skin glands ofAustralian tree frogs, Litoria caerulea and Litoriagenimaculata. NMR spectroscopy was used to observe changesinduced by these peptides in the 31P resonances of bacterialmembranes in vivo. Caerin 1.1 and maculatin 1.1, both wide-spectrum antibiotics, disrupted the membranes ofBacillus cereus and Staphylococcus epidermidis (Gram-positive), leadingto an increase in the isotropic 31P NMR signal. Caerin 4.1, anarrow-spectrum antibiotic, however, did not affect the 31Pspectra of these organisms. The results demonstrate the use of31P NMR to study the effects of membrane-disrupting agents onthe membranes of live bacteria. |
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| Keywords: | antimicrobial peptide Bacillus cereus bacterial membrane Staphylococcus epidermidis 31P NMR |
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