This Article Full Text Full Text (PDF) All Versions of this Article: biophysj.105.067678v1 89/4/2434    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Dave, P. C. Articles by Straus, S. K. Search for Related Content PubMed PubMed Citation Articles by Dave, P. C. Articles by Straus, S. K.

Interaction of Alamethicin with Ether-Linked Phospholipid Bilayers: Oriented Circular Dichroism, ³¹P Solid-State NMR, and Differential Scanning Calorimetry Studies

Department of Chemistry, University of British Columbia, Vancouver, British Columbia V6T 1Z1, Canada

Correspondence: Address reprint requests to Suzana K. Straus, Tel.: 604-822-2537; Fax: 604-822-2157; E-mail: sstraus{at}chem.ubc.ca.

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.

This article has been cited by other articles:

				Y.-L. Pan, J. T.-J. Cheng, J. Hale, J. Pan, R. E. W. Hancock, and S. K. Straus Characterization of the Structure and Membrane Interaction of the Antimicrobial Peptides Aurein 2.2 and 2.3 from Australian Southern Bell Frogs Biophys. J., April 15, 2007; 92(8): 2854 - 2864. [Abstract] [Full Text] [PDF]