Interaction of antimicrobial peptides from Australian amphibians with lipid membranes |
| |
Authors: | Marcotte Isabelle Wegener Kate L Lam Yuen-Han Chia Brian C S de Planque Maurits R R Bowie John H Auger Michèle Separovic Frances |
| |
Affiliation: | Département de Chimie, Centre de Recherche en Sciences et en Ingénierie des Macromolécules, Université Laval, Québec, Québec, Canada G1K 7P4. |
| |
Abstract: | Solid-state NMR and CD spectroscopy were used to study the effect of antimicrobial peptides (aurein 1.2, citropin 1.1, maculatin 1.1 and caerin 1.1) from Australian tree frogs on phospholipid membranes. 31P NMR results revealed some effect on the phospholipid headgroups when the peptides interact with DMPC/DHPC (dimyristoylphosphatidylcholine/dihexanoylphosphatidylcholine) bicelles and aligned DMPC multilayers. 2H NMR showed a small effect of the peptides on the acyl chains of DMPC in bicelles or aligned multilayers, suggesting interaction with the membrane surface for the shorter peptides and partial insertion for the longer peptides. 15N NMR of selectively labelled peptides in aligned membranes and oriented CD spectra indicated an alpha-helical conformation with helix long axis approximately 50 degrees to the bilayer surface at high peptide concentrations. The peptides did not appear to insert deeply into PC membranes, which may explain why these positively charged peptides preferentially lyse bacterial rather than eucaryotic cells. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|