Proline-15 creates an amphipathic wedge in maculatin 1.1 peptides that drives lipid membrane disruption》.pdf

Biochimica et Biophysica Acta 1848 (2015) 2277–2289 Contents lists available at ScienceDirect Biochimica et Biophysica Acta journal h omepage: /locate/bbamem Proline-15 creates an amphipathic wedge in maculatin 1.1 peptides that drives lipid membrane disruption Marc-Antoine Sani a,1, Tzong-Hsien Lee b,1, Marie-Isabel Aguilar b,⁎, Frances Separovic a,⁎ a School of Chemistry, Bio21 Institute, University of Melbourne, VIC 3010, Australia b Department of Biochemistry and Molecular Biology, Monash University, Clayton, VIC 3800, Australia a r t i c l e i n f o a b s t r a c t Article history: The membrane interaction of peptides derived from maculatin 1.1 and caerin 1.1, with the sequence motif of N Received 24 April 2015 and C termini of maculatin 1.1, was compared in order to understand the role of these common sequence motifs, Received in revised form 5 June 2015 which encompass critical proline residues, on peptide secondary structure and on membrane binding and Accepted 11 June 2015 disruption in zwitterionic and anionic membranes. The peptides incorporated a single substitution with lysine Available online 14 June 2015 or deletion of the central region to mimic the length of the antimicrobial peptides, citropin 1.1 and aurein 1.2. Keywords: The impact of these changes in the sequence, length and physicochemical properties, on lytic activity and struc- Antimicrobial peptide ture was as