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The oblique insertion of type 1 viral fusion peptides into the cell membrane of the host cell has been shown previously to be an essential element of viral fusion. The actual physical explanation of the cause of the oblique insertion has been the subject of speculation. In this study the physical properties of the fusion peptide surface have been determined computationally and compared to the tilt angles determined both experimentally and by the use of molecular dynamics. It has been shown that the relationship between the distribution of lipophilic potential over the peptide surface and the peptide geometry control the tilt angle of the peptide in a biomimetic DMPC bilayer whereas the depth of penetration into the bilayer appears to be determined by the electrostatic potential and hydrogen bonding at the C-terminus.

Original publication

DOI

10.1007/s00249-010-0611-1

Type

Journal article

Journal

Eur Biophys J

Publication Date

10/2010

Volume

39

Pages

1537 - 1545

Keywords

Amino Acid Sequence, Cell Membrane, Dimyristoylphosphatidylcholine, Hydrophobic and Hydrophilic Interactions, Lipid Bilayers, Molecular Dynamics Simulation, Molecular Sequence Data, Peptide Fragments, Protein Conformation, Static Electricity, Viral Fusion Proteins, Virus Internalization, Viruses