The University of Southampton
University of Southampton Institutional Repository

Interaction of antimicrobial peptides from Australian amphibians with lipid membranes

Interaction of antimicrobial peptides from Australian amphibians with lipid membranes
Interaction of antimicrobial peptides from Australian amphibians with lipid membranes
Solid-state NMR and CD spectroscopy were used to study the effect of antimicrobial peptides (aurein 1.2, citropin 1.1, maculatin 1.1 and caerin 1.1) from Australian tree frogs on phospholipid membranes. 31P NMR results revealed some effect on the phospholipid headgroups when the peptides interact with DMPC/DHPC (dimyristoylphosphatidylcholine/dihexanoylphosphatidylcholine) bicelles and aligned DMPC multilayers. 2H NMR showed a small effect of the peptides on the acyl chains of DMPC in bicelles or aligned multilayers, suggesting interaction with the membrane surface for the shorter peptides and partial insertion for the longer peptides. 15N NMR of selectively labelled peptides in aligned membranes and oriented CD spectra indicated an ?-helical conformation with helix long axis 50° to the bilayer surface at high peptide concentrations. The peptides did not appear to insert deeply into PC membranes, which may explain why these positively charged peptides preferentially lyse bacterial rather than eucaryotic cells.
Antimicrobial peptides, Lipid membranes, Structure, Lysis, NMR, CD
0009-3084
107-120
Marcotte, I
40b938d0-d18d-4b94-b1da-37b053db7808
Wegener, K L
b6533adf-04bb-4f74-ac68-1d55add7f219
Lam, Y H
89f4e731-8ae8-4de9-8c7d-8166857e845f
Chia, B C S
82aefe64-f1e5-4646-a1ce-2a308049a3e1
de Planque, M R R
a1d33d13-f516-44fb-8d2c-c51d18bc21ba
Bowie, J H
b4803257-fdb8-41a6-be47-a3dde3d2fa2f
Auger, M
125d3d26-6833-4bad-a804-9366a622f976
Separovic, F
1ca03f7a-0a45-465f-a683-33928d272fcd
Marcotte, I
40b938d0-d18d-4b94-b1da-37b053db7808
Wegener, K L
b6533adf-04bb-4f74-ac68-1d55add7f219
Lam, Y H
89f4e731-8ae8-4de9-8c7d-8166857e845f
Chia, B C S
82aefe64-f1e5-4646-a1ce-2a308049a3e1
de Planque, M R R
a1d33d13-f516-44fb-8d2c-c51d18bc21ba
Bowie, J H
b4803257-fdb8-41a6-be47-a3dde3d2fa2f
Auger, M
125d3d26-6833-4bad-a804-9366a622f976
Separovic, F
1ca03f7a-0a45-465f-a683-33928d272fcd

Marcotte, I, Wegener, K L, Lam, Y H, Chia, B C S, de Planque, M R R, Bowie, J H, Auger, M and Separovic, F (2003) Interaction of antimicrobial peptides from Australian amphibians with lipid membranes. Chemistry and Physics of Lipids, 122 (1-2), 107-120. (doi:10.1016/S009-3084(02)00182-2).

Record type: Article

Abstract

Solid-state NMR and CD spectroscopy were used to study the effect of antimicrobial peptides (aurein 1.2, citropin 1.1, maculatin 1.1 and caerin 1.1) from Australian tree frogs on phospholipid membranes. 31P NMR results revealed some effect on the phospholipid headgroups when the peptides interact with DMPC/DHPC (dimyristoylphosphatidylcholine/dihexanoylphosphatidylcholine) bicelles and aligned DMPC multilayers. 2H NMR showed a small effect of the peptides on the acyl chains of DMPC in bicelles or aligned multilayers, suggesting interaction with the membrane surface for the shorter peptides and partial insertion for the longer peptides. 15N NMR of selectively labelled peptides in aligned membranes and oriented CD spectra indicated an ?-helical conformation with helix long axis 50° to the bilayer surface at high peptide concentrations. The peptides did not appear to insert deeply into PC membranes, which may explain why these positively charged peptides preferentially lyse bacterial rather than eucaryotic cells.

Full text not available from this repository.

More information

Published date: 2003
Keywords: Antimicrobial peptides, Lipid membranes, Structure, Lysis, NMR, CD
Organisations: Nanoelectronics and Nanotechnology

Identifiers

Local EPrints ID: 264694
URI: http://eprints.soton.ac.uk/id/eprint/264694
ISSN: 0009-3084
PURE UUID: c868835d-22f3-449f-a8f5-b58707c4e335
ORCID for M R R de Planque: ORCID iD orcid.org/0000-0002-8787-0513

Catalogue record

Date deposited: 17 Oct 2007
Last modified: 17 Dec 2019 01:43

Export record

Altmetrics

Contributors

Author: I Marcotte
Author: K L Wegener
Author: Y H Lam
Author: B C S Chia
Author: M R R de Planque ORCID iD
Author: J H Bowie
Author: M Auger
Author: F Separovic

University divisions

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×