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Interactions of the Antimicrobial Peptide Maculatin 1.1 and Analogues with Phospholipid Bilayers

David I. Fernandez A , Marc-Antoine Sani A and Frances Separovic A B
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A School of Chemistry, Bio21 Institute, University of Melbourne, Melbourne, Vic. 3010, Australia.

B Corresponding author. Email: fs@unimelb.edu.au




Professor Frances Separovic is a Biophysical Chemist who is Head of the School of Chemistry, University of Melbourne, and was Assistant Dean (EO) (2001–02) and Associate Dean (2009–10) of the Faculty of Science. Frances has developed solid-state NMR techniques to determine the structure and dynamics of membrane components in situ, specializing in peptide antibiotics and toxins within phospholipid membranes and was awarded the Robertson Medal by the Australian Society for Biophysics in 2009. As well as serving as General Treasurer of the Royal Australian Chemical Institute (2008–10), she was elected to Council of the Biophysical Society (USA) for 2007–10; Treasurer of Lorne Protein Conference (2006–09), Council of International Union of Pure and Applied Biophysics, IUPAB (2002–05); President of the Australian Society for Biophysics (1999–2001); Director of Australian New Zealand Magnetic Resonance Society (1996–2000, 2010–); and an editorial board member of Concepts in Magnetic Resonance, Biochimica Biophysica Acta – Biomembranes and Accounts in Chemical Research.

Australian Journal of Chemistry 64(6) 798-805 https://doi.org/10.1071/CH11062
Submitted: 4 February 2011  Accepted: 17 March 2011   Published: 27 June 2011



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Proline Facilitates Membrane Insertion of the Antimicrobial Peptide Maculatin 1.1 via Surface Indentation and Subsequent Lipid Disordering
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Effect of phosphatidylcholine bilayer thickness and molecular order on the binding of the antimicrobial peptide maculatin 1.1
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Copper Modulation of Amyloid Beta 42 Interactions with Model Membranes
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Charged Antimicrobial Peptides Can Translocate across Membranes without Forming Channel-like Pores
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Structural effects of the antimicrobial peptide maculatin 1.1 on supported lipid bilayers
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