Membrane binding and perturbation studies of the antimicrobial peptides caerin, citropin and maculatin

Chia, C. S. Brian, Gong, Yujing, Bowie, John H., Zuegg, Johannes and Cooper, Matthew A. (2011) Membrane binding and perturbation studies of the antimicrobial peptides caerin, citropin and maculatin. Peptide Science, 96 2: 147-157. doi:10.1002/bip.21438

Author Chia, C. S. Brian
Gong, Yujing
Bowie, John H.
Zuegg, Johannes
Cooper, Matthew A.
Title Membrane binding and perturbation studies of the antimicrobial peptides caerin, citropin and maculatin
Journal name Peptide Science   Check publisher's open access policy
ISSN 0006-3525
Publication date 2011
Year available 2010
Sub-type Article (original research)
DOI 10.1002/bip.21438
Volume 96
Issue 2
Start page 147
End page 157
Total pages 11
Editor Joel P. Schneider
Place of publication New York, NY, U.S.A.
Publisher John Wiley & Sons
Collection year 2011
Language eng
Abstract Citropin 1.1, Maculatin 1.1 and Caerin 1.1 are short antibacterial cationic peptides from the skin glands of the Australian tree frog Litoria species. Several analogues have been synthesized to give a better insight into the relationship between the structure of the peptides and their antibacterial and haemolytic activity. Binding studies using a surface plasmon resonance (SPR) biosensor together with a vesicle-capture sensor chip have been used to investigate selectivity of the peptides and their analogues for 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol (DMPG) and 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) vesicles, as well as for vesicles made from lipid extracts from Escherichia coli and bovine brain. Data obtained for membrane selectivity using natural lipid extracts show better correlation with MIC values against Gram-positive bacteria and haemolytic activity than that obtained using synthetic DMPG and DMPC. Electron microscopy and membrane leakage studies using Gram-positive bacteria gave further insight into the membrane disruption properties of the peptides. For Maculatin 1.1, it was found that the central proline residue, which is responsible for a bend in the α-helical structure, is essential not only for the antibacterial activity, but also for binding to, and perturbation of membranes. The Caerin analogues showed only small variations in their MIC values and membrane binding. In contrast, for Citropin 1.1, the analogue replacing the aspartate with a lysine showed the lowest MIC against Gram-positive bacteria and best membrane binding to E. coli lipid extracts, coinciding with an increased hydrophobic moment of the peptide. These data give further insight into these anti-microbial natural products, towards the development and evaluation of these and other analogues as potential antibiotics. © 2010 Wiley Periodicals, Inc. Biopolymers (Pept Sci), 2010
Keyword Anti-microbial peptides
Peptide antibiotic
Electron microscopy
Membrane selectivity
Surface plasmon resonance
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Article first published online: 21 August, 2010; no month nted on print version. Special Issue: The Eighth Australian Peptide Conference: Peptides - Tools, Targets and Therapeutics

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2011 Collection
Institute for Molecular Bioscience - Publications
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 8 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 12 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Fri, 04 Feb 2011, 11:39:09 EST by Susan Allen on behalf of Institute for Molecular Bioscience