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Peptide-induced fusion-fragmentation

Lipid phases diagrams, peptide-induced fusion-fragmentation... [Pg.120]

Facial amphiphilic peptides are another class of facial amphiphiles, which play an important rote in many biological processes involving lipid bilayer membranes. Because of the large surface area of the amphiphilic domains, they are prone to interact with the hydrophiUc/hydrophobic interface of lipid bilayers, which is necessary to assist in membrane fusion or transmembrane pore formation. In the case of pore-forming antibiotics, the peptides are often relatively small (between 25 and 100 amino acids) and the entire peptide becomes facially amphiphilic on folding into the secondary structure. In the case of membrane fusion or curvature-inducing proteins only the peptide fragment, which interacts with the bilayer membrane, is facially amphiphilic. [Pg.2706]


See other pages where Peptide-induced fusion-fragmentation is mentioned: [Pg.289]    [Pg.121]    [Pg.18]    [Pg.59]    [Pg.416]    [Pg.260]    [Pg.96]    [Pg.306]    [Pg.859]    [Pg.96]    [Pg.306]    [Pg.497]    [Pg.572]    [Pg.326]   


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