Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/17961
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dc.contributor.authorBalla, M.-
dc.contributor.authorBowie, J.-
dc.contributor.authorSeparovic, F.-
dc.date.issued2004-
dc.identifier.citationEuropean Biophysics Journal, 2004; 33(2):109-116-
dc.identifier.issn0175-7571-
dc.identifier.issn1432-1017-
dc.identifier.urihttp://hdl.handle.net/2440/17961-
dc.descriptionThe original publication is available at www.springerlink.com-
dc.description.abstractAntimicrobial peptides, isolated from the dorsal glands of Australian tree frogs, possess a wide spectrum of biological activity and some are specific to certain pathogens. These peptides have the capability of disrupting bacterial membranes and lysing lipid bilayers. This study focused on the following amphibian peptides: (1) aurein 1.2, a 13-residue peptide; (2) citropin 1.1, with 16 residues; and (3) maculatin 1.1, with 21 residues. The antibiotic activity and structure of these peptides have been studied and compared and possible mechanisms by which the peptides lyse bacterial membrane cells have been proposed. The peptides adopt amphipathic alpha-helical structures in the presence of lipid micelles and vesicles. Specifically 15N-labelled peptides were studied using solid-state NMR to determine their structure and orientation in model lipid bilayers. The effect of these peptides on phospholipid membranes was determined by 2H and 31P solid-state NMR techniques in order to understand the mechanisms by which they exert their biological effects that lead to the disruption of the bacterial cell membrane. Aurein 1.2 and citropin 1.1 are too short to span the membrane bilayer while the longer maculatin 1.1, which may be flexible due to the central proline, would be able to span the bilayer as a transmembrane alpha-helix. All three peptides had a peripheral interaction with phosphatidylcholine bilayers and appear to be located in the aqueous region of the membrane bilayer. It is proposed that these antimicrobial peptides have a "detergent"-like mechanism of membrane lysis.-
dc.description.statementofresponsibilityM. S. Balla, J. H. Bowie and F. Separovic-
dc.language.isoen-
dc.publisherSpringer-Verlag-
dc.rightsCopyright © EBSA 2003-
dc.subjectAnimals-
dc.subjectRanidae-
dc.subjectChromones-
dc.subjectLipid Bilayers-
dc.subjectPhospholipids-
dc.subjectAntimicrobial Cationic Peptides-
dc.subjectAmphibian Proteins-
dc.subjectMembrane Proteins-
dc.subjectMembranes, Artificial-
dc.subjectMagnetic Resonance Spectroscopy-
dc.subjectMembrane Fluidity-
dc.subjectProtein Conformation-
dc.titleSolid-state NMR study of antimicrobial peptides from Australian frogs in phospholipid membranes-
dc.typeJournal article-
dc.identifier.doi10.1007/s00249-003-0342-7-
pubs.publication-statusPublished-
Appears in Collections:Aurora harvest 2
Chemistry publications

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