Proline facilitates membrane insertion of the antimicrobial peptide maculatin 1.1 via surface indentation and subsequent lipid disordering

DI Fernandez; TH Lee; MA Sani; MI Aguilar; F Separovic

Journal article

Proline facilitates membrane insertion of the antimicrobial peptide maculatin 1.1 via surface indentation and subsequent lipid disordering

DI Fernandez, TH Lee, MA Sani, MI Aguilar, F Separovic

Biophysical Journal | CELL PRESS | Published : 2013

DOI: 10.1016/j.bpj.2013.01.059

Abstract

The role of proline in the disruption of membrane bilayer structure upon antimicrobial peptide (AMP) binding was studied. Specifically, 31P and 2H solid-state NMR and dual polarization interferometry (DPI) were used to analyze the membrane interactions of three AMPs: maculatin 1.1 and two analogs in which Pro-15 is replaced by Gly and Ala. For NMR, deuterated dimyristoylphosphatidylcholine (d54-DMPC) and d54-DMPC/ dimyristoylphosphatidylglycerol (DMPG) were used to mimic eukaryotic and prokaryotic membranes, respectively. In fluid-phase DMPC bilayer systems, the peptides interacted primarily with the bilayer surface, with the native peptide having the strongest interaction. In the mixed DMPC..

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University of Melbourne Researchers

Marco Sani Author

Frances Separovic Author

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Grants

Funding Acknowledgements

D.I.F. received an Albert Shimmins Postgraduate Writing-Up Award from the University of Melbourne and an Australian Postgraduate Award. M.I.A. and F.S. received financial support from the Australian Research Council.