Studies on viral fusion peptides: the distribution of lipophilic and electrostatic potential over the peptide determines the angle of insertion into a membrane.
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.
Taylor
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A
Department of Biochemistry, University of Oxford, South Parks Rd, Oxford OX1 3QU, UK. alan.taylor@stx.oxon.org
Sansom
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MS
D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000378:metabolism*; D004134:Dimyristoylphosphatidylcholine / Q000378:metabolism; D057927:Hydrophobic and Hydrophilic Interactions; D008051:Lipid Bilayers / Q000378:metabolism; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D055672:Static Electricity; D014760:Viral Fusion Proteins / Q000737:chemistry* / Q000378:metabolism; D053586:Virus Internalization; D014780:Viruses / Q000378:metabolism
D008051:Lipid Bilayers; D010446:Peptide Fragments; D014760:Viral Fusion Proteins; D004134:Dimyristoylphosphatidylcholine