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- W2063737329 endingPage "338" @default.
- W2063737329 startingPage "319" @default.
- W2063737329 abstract "The amphipathic helix, in which hydrophobic and hydrophilic residues are grouped on opposing faces, is a structural motif found in many peptides and proteins that bind to membranes. One of the physical properties of membranes that can be altered by the binding of amphipathic helices is membrane monolayer curvature strain. Class A amphipathic helices, which are present in exchangeable plasma lipoproteins, can stabilize membranes by reducing negative monolayer curvature strain; proline-punctuated class A amphipathic helical segments are particularly effective in this regard. This property is suggested to be associated with some of the beneficial biological effects of this protein. On the other hand, lytic amphipathic helical peptides can act by increasing negative curvature strain or by forming pores composed of helical clusters. Thus, different amphipathic helical peptides can be membrane stabilizing or be lytic to membranes, depending on the structural motif of the helix, which in turn determines the nature of its association with membranes. Features of these peptides that are responsible for their specific properties are discussed." @default.
- W2063737329 created "2016-06-24" @default.
- W2063737329 creator A5008312902 @default.
- W2063737329 creator A5030953137 @default.
- W2063737329 creator A5051686775 @default.
- W2063737329 creator A5077610815 @default.
- W2063737329 date "1995-01-01" @default.
- W2063737329 modified "2023-10-17" @default.
- W2063737329 title "Mechanisms for the modulation of membrane bilayer properties by amphipathic helical peptides" @default.
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