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Biophys J, February 2001, p. 643-655, Vol. 80, No. 2

Implicit Solvent Model Studies of the Interactions of the Influenza Hemagglutinin Fusion Peptide with Lipid Bilayers

Dalit Bechor and Nir Ben-Tal

Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv 69978, Israel

The "fusion peptide," a segment of ~20 residues of the influenza hemagglutinin (HA), is necessary and sufficient for HA-induced membrane fusion. We used mean-field calculations of the free energy of peptide-membrane association (Delta Gtot) to deduce the most probable orientation of the fusion peptide in the membrane. The main contributions to Delta Gtot are probably from the electrostatic (Delta Gel) and nonpolar (Delta Gnp) components of the solvation free energy; these were calculated using continuum solvent models. The peptide was described in atomic detail and was modeled as an alpha -helix based on spectroscopic data. The membrane's hydrocarbon region was described as a structureless slab of nonpolar medium embedded in water. All the helix-membrane configurations, which were lower in Delta Gtot than the isolated helix in the aqueous phase, were in the same (wide) basin in configurational space. In each, the helix was horizontally adsorbed at the water-bilayer interface with its principal axis parallel to the membrane plane, its hydrophobic face dissolved in the bilayer, and its polar face in the water. The associated Delta Gtot value was ~-8 to -10 kcal/mol (depending on the rotameric state of one of the phenylalanine residues). In contrast, the Delta Gtot values associated with experimentally observed oblique orientations were found to be near zero, suggesting they are marginally stable at best. The theoretical model did not take into account the interactions of the polar headgroups with the peptide and peptide-induced membrane deformation effects. Either or both may overcompensate for the Delta Gtot difference between the horizontal and oblique orientations.

Biophys J, February 2001, p. 643-655, Vol. 80, No. 2
© 2001 by the Biophysical Society   0006-3495/01/02/643/13  $2.00


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