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Biophysical Journal 87:14-22 (2004)
© 2004 The Biophysical Society

Bilayer Conformation of Fusion Peptide of Influenza Virus Hemagglutinin: A Molecular Dynamics Simulation Study

Qiang Huang * {dagger}, Cheng-Lung Chen * and Andreas Herrmann {dagger}

* Department of Chemistry, National Sun Yat-sen University, Kaohsiung, Taiwan, Republic of China; and {dagger} Institute of Biology, Molecular Biophysics, Humboldt-University Berlin, 10115 Berlin, Germany

Correspondence: Address reprint requests to Andreas Herrmann, Humboldt-University Berlin, Institute of Biology/Molecular Biophysics, Invalidenstr. 43, D-10115 Berlin, Germany. Tel.: 49-30-2093-8830; Fax: 49-30-2093-8585; E-mail: andreas.herrmann{at}rz.hu-berlin.de.

Unraveling the conformation of membrane-bound viral fusion peptides is essential for understanding how those peptides destabilize the bilayer topology of lipids that is important for virus-cell membrane fusion. Here, molecular dynamics (MD) simulations were performed to investigate the conformation of the 20 amino acids long fusion peptide of influenza hemagglutinin of strain X31 bound to a dimyristoyl phosphatidylcholine (DMPC) bilayer. The simulations revealed that the peptide adopts a kinked conformation, in agreement with the NMR structures of a related peptide in detergent micelles. The peptide is located at the amphipathic interface between the headgroups and hydrocarbon chains of the lipid by an energetically favorable arrangement: The hydrophobic side chains of the peptides are embedded into the hydrophobic region and the hydrophilic side chains are in the headgroup region. The N-terminus of the peptide is localized close to the amphipathic interface. The molecular dynamics simulations also revealed that the peptide affects the surrounding bilayer structure. The average hydrophobic thickness of the lipid phase close to the N-terminus is reduced in comparison with the average hydrophobic thickness of a pure dimyristoyl phosphatidylcholine bilayer.




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