Interaction of alamethicin with ether-linked phospholipid bilayers: oriented circular dichroism, 31P solid-state NMR, and differential scanning calorimetry studies.
The arrangement of the antimicrobial peptide alamethicin was studied by oriented circular dichroism, 31P solid-state NMR, and differential scanning calorimetry in ether-linked phospholipid bilayers composed of 1,2-O-dihexadecyl-sn-glycero-3-phosphocholine (DHPC). The measurements were performed as a function of alamethicin concentration relative to the lipid concentration, and results were compared to those reported in the literature for ester-linked phospholipid bilayers. At ambient temperature, alamethicin incorporates into the hydrophobic core of DHPC bilayers but results in more lipid disorder than observed for ester-linked 1-palmitoyl, 2-oleoyl-sn-glycero-3-phosphatidylcholine (POPC) lipid bilayers. This orientational disorder appears to depend on lipid properties such as bilayer thickness. Moreover, the results suggest that alamethicin inserts into the hydrophobic core of the bilayers (at high peptide concentration) for both ether- and ester-linked lipids but using a different mechanism, namely toroidal for DHPC and barrel-stave for POPC.
Dave
Paresh C
PC
Department of Chemistry, University of British Columbia, Vancouver, British Columbia V6T 1Z1, Canada.
Billington
Emma
E
Pan
Yeang-Ling
YL
Straus
Suzana K
SK
D000408:Alamethicin / Q000737:chemistry*; D002152:Calorimetry, Differential Scanning / Q000379:methods; D002942:Circular Dichroism / Q000379:methods; D004986:Ether / Q000737:chemistry*; D007473:Ion Channels / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008560:Membrane Fluidity; D008565:Membrane Proteins / Q000737:chemistry*; D010743:Phospholipids / Q000737:chemistry*; D010759:Phosphorus Isotopes
D007473:Ion Channels; D008051:Lipid Bilayers; D008565:Membrane Proteins; D010743:Phospholipids; D010759:Phosphorus Isotopes; D004986:Ether; D000408:Alamethicin