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- W1981671135 endingPage "1544" @default.
- W1981671135 startingPage "1537" @default.
- W1981671135 abstract "Physical properties of membranes, such as fluidity, charge or curvature influence their function. Proteins and peptides can modulate those properties and conversely, the lipids can affect the activity and/or the structure of the former. Tilted peptides are short hydrophobic protein fragments characterized by an asymmetric distribution of their hydrophobic residues when helical. They were detected in viral fusion proteins and in proteins involved in different biological processes that need membrane destabilization. Those peptides and non lamellar lipids such as PE or PA appear to cooperate in the lipid destabilization process by enhancing the formation of negatively-curved domains. Such highly bent lipidic structures could favour the formation of the viral fusion pore intermediates or that of toroidal pores. Structural flexibility appears as another crucial property for the interaction of peptides with membranes. Computational analysis on another kind of lipid-interacting peptides, i.e. cell penetrating peptides (CPP) suggests that peptides being conformationally polymorphic should be more prone to traverse the bilayer. Future investigations on the structural intrinsic properties of tilted peptides and the influence of CPP on the bilayer organization using the techniques described in this chapter should help to further understand the molecular determinants of the peptide/lipid inter-relationships." @default.
- W1981671135 created "2016-06-24" @default.
- W1981671135 creator A5005129801 @default.
- W1981671135 creator A5050533193 @default.
- W1981671135 creator A5055176983 @default.
- W1981671135 creator A5072207276 @default.
- W1981671135 date "2008-07-01" @default.
- W1981671135 modified "2023-09-27" @default.
- W1981671135 title "Relationships between the orientation and the structural properties of peptides and their membrane interactions" @default.
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