Studies on viral fusion peptides: the distribution of lipophilic and electrostatic potential over the peptide determines the angle of insertion into a membrane.

Journal article

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 th...

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Authors: Taylor, A; Sansom, MS

• Publication status: Published
• Journal: European biophysics journal : EBJ
• Volume: 39
• Issue: 11
• Pages: 1537-1545
• Publication date: 2010-10-01
• DOI: 10.1007/s00249-010-0611-1
• EISSN: 1432-1017
• ISSN: 0175-7571
• Language: English
• Keywords: Amino Acid Sequence; Dimyristoylphosphatidylcholine; Molecular Sequence Data; Protein Conformation; Static Electricity; Viral Fusion Proteins; Virus Internalization; Peptide Fragments; Lipid Bilayers; Viruses; Molecular Dynamics Simulation; Hydrophobic and Hydrophilic Interactions; Cell Membrane