Gramicidin channel-induced lipid membrane deformation energy: influence of chain length and boundary conditions.
The influence of boundary conditions on the deformation energy of a lipid membrane containing a gramicidin A channel was evaluated numerically. A liquid crystal model was used to calculate the relative contributions of compression, splay and surface tension. It is proposed that the nearest neighbor lipid molecules are displaced from the channel end in a direction perpendicular to the bilayer and it is concluded that surface tension is the major component of the deformation free energy for monoolein (gmo)/n-alkane membranes. This unexpected result supports the validity of the liquid crystal models of membrane deformation since gramicidin lifetime has been shown to correlate with surface tension for gmo membranes. The theory accurately predicts the experimentally measured relative lifetimes without the use of adjustable parameters. For conditions where splay may be neglected surface tension is always the major component of the deformation energy, irrespective of the magnitude of the compression coefficient. The deformation may extend for hundreds of angstroms from the peptide. The results obtained here are expected to be important for the characterization of protein-membrane interactions in general.
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Department of Physiology and Medical Biophysics, Biomedical Centre, Uppsala, Sweden.
D006096:Gramicidin / Q000737:chemistry*; D007473:Ion Channels / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry*; D013500:Surface Tension; D013816:Thermodynamics
D007473:Ion Channels; D008051:Lipid Bilayers; D006096:Gramicidin