Chapter 6 Modulation of Lipid Polymorphism by Peptides
Current topics in membranesPublished 1 January 1997
Richard M. Epand
Citations21
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TL;DR
This suggestion that the fusogenic segments of viral fusion proteins may initiate membrane fusion by destabilizing the bilayer of target membranes is supported by the findings that many bilayerstabilizing peptides and proteins are found to be inhibitors of viral infectivity and syncytia formation.
Abstract
Certain peptides have a marked effect on membrane polymorphism. Some of these effects can be rationalized in terms of the motionally averaged cross-sectional area of the peptide-lipid complex in the center of the bilayer versus that at the water-membrane interface. A number of factors determine this shape property, including peptide hydrophobicity, the location of the peptide in a membrane, the presence of amino acids such as Lys that contain several single C-C bonds in the side chain, or the location of bulky amino acid residues such as Trp, as well as the conformation of the peptide. Modulation of lipid polymorphism may be related to certain membrane functions. For example, the fusogenic segments of viral fusion proteins may initiate membrane fusion by destabilizing the bilayer of target membranes. This suggestion is further supported by the findings that many bilayerstabilizing peptides and proteins are found to be inhibitors of viral infectivity and syncytia formation.
Keywords
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