Journal article
Interactions of the antimicrobial peptide maculatin 1.1 and analogues with phospholipid bilayers
DI Fernandez, MA Sani, F Separovic
Australian Journal of Chemistry | CSIRO PUBLISHING | Published : 2011
DOI: 10.1071/CH11062
Abstract
The interactions of the antimicrobial peptide, maculatin 1.1 (GLFGVLAKVAAHVVPAIAEHF-NH2) and two analogues, with model phospholipid membranes have been studied using solid-state NMR and circular dichroism spectroscopy. Maculatin 1.1 and the P15G and P15A analogues displayed minimal secondary structure in water, but with zwitterionic dimyristoylphosphatidylcholine (DMPC) vesicles displayed a significant increase in α-helical content. In mixed phospholipid vesicles of DMPC and anionic dimyristoylphosphatidylglycerol (DMPG), each peptide was highly structured with ∼80%-helical content. In DMPC vesicles, the native peptide displayed moderate head group interaction and significant perturbation of..
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Funding Acknowledgements
D.I.F. is the recipient of an Australian Postgraduate Award. The authors thank Dr J. D. Gehman (University of Melbourne) for his valuable assistance in deconvoluting and dePaking of NMR spectra. F.S. thanks Dr A. Miles (Birkbeck College, UK) for his assistance with CD spectroscopy and acknowledges the Melbourne Research Grant Scheme for financial support.