European Biophysics Journal

, Volume 33, Issue 2, pp 109–116 | Cite as

Solid-state NMR study of antimicrobial peptides from Australian frogs in phospholipid membranes

  • M. S. Balla
  • J. H. Bowie
  • F. SeparovicEmail author


Antimicrobial 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 α-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 α-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.


Antibiotics Bilayers Membranes Peptides Solid-state NMR 



M.S.B. is grateful to the University of Melbourne for award of an MRS scholarship. J.H.B. and F.S. are grateful to the ARC for financial support.


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Copyright information

© EBSA 2004

Authors and Affiliations

  1. 1.School of ChemistryUniversity of MelbourneAustralia
  2. 2.Department of ChemistryUniversity of AdelaideAustralia

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