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

¹ University of British Columbia

^* To whom correspondence should be addressed. E-mail: sstraus{at}chem.ubc.ca.

Submitted on May 30, 2005
Revised on June 21, 2005
Accepted on 18 July 2005

	Abstract

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 (1-5). At ambient temperature, alamethicin incorporates into the hydrophobic core of DHPC bilayers, but results in more lipid disorder than observed for ester-linked 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.

Key Words: alamethicin, differential scanning calorimetry, oriented circular dichroism, solid state NMR, toroidal model

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