Biophysical studies of membrane proteins/peptides. Interaction with ...
Biophysical studies of membrane proteins/peptides. Interaction with ...
Biophysical studies of membrane proteins/peptides. Interaction with ...
Create successful ePaper yourself
Turn your PDF publications into a flip-book with our unique Google optimized e-Paper software.
INTRODUCTION: LIPID-PROTEIN INTERACTIONS<br />
However, this proposed mechanism for sorting <strong>of</strong> <strong>membrane</strong> <strong>proteins</strong> is still<br />
controversial (Mouritsen, 2005).<br />
Concerning <strong>membrane</strong> protein partition to specific regions <strong>of</strong> the bilayer, <strong>of</strong><br />
particular interest is the possibility that certain <strong>membrane</strong> <strong>proteins</strong> prefer insertion in the<br />
boundaries between lipid phases in the <strong>membrane</strong>s. These boundaries present a higher<br />
probability <strong>of</strong> lipid packing defects that can be used by certain <strong>proteins</strong> to access deeper<br />
regions in the <strong>membrane</strong> (Pérez-Gil et al., 2005).<br />
2.10. Lipid sorting by <strong>proteins</strong> and formation <strong>of</strong><br />
lipid domains<br />
The presence <strong>of</strong> very stable lipid domains in the <strong>membrane</strong> is only expected if the<br />
free energies for interaction between phase separated lipids is very high. In<br />
bio<strong>membrane</strong>s this is rarely the case, and therefore lateral structures that arise must have<br />
a reasonably dynamical nature. In model <strong>membrane</strong>s, the differences in free-energies<br />
for lipid-lipid interactions are typically on the order <strong>of</strong> a few calories per mole. In<br />
contrast, the free-energies involved in protein-lipid interactions are much larger<br />
(Hinderliter et al., 2001). Therefore <strong>membrane</strong> <strong>proteins</strong> when incorporated in lipid<br />
<strong>membrane</strong>s can contribute decisively to the final lipid phase equilibria.<br />
In the presence <strong>of</strong> a multicomponent lipid mixture in the fluid phase, insertion <strong>of</strong> a<br />
<strong>membrane</strong> protein can lead, as already described, to enrichment <strong>of</strong> one <strong>of</strong> the lipid<br />
species around the protein due to more efficient packing in the protein-lipid interface.<br />
This preferential association can stabilize a lipid phase around the protein, even under<br />
conditions where it is metastable in the protein-free system. This preferred phase is said<br />
to wet the protein (Gil et al., 1998). The wetting layer <strong>of</strong> lipids only extends over a<br />
finite (nonmacroscopic) distance. Theoretical <strong>studies</strong> have predicted that effects on<br />
lipids by inclusion <strong>of</strong> <strong>proteins</strong> may extend up to 20 lipid shells around the protein (Fattal<br />
and Ben-Shaul, 1993; Sperotto and Mouritsen, 1991), and results from some<br />
experimental <strong>studies</strong> were rationalized on the basis <strong>of</strong> wetting <strong>of</strong> <strong>membrane</strong> <strong>proteins</strong> and<br />
formation <strong>of</strong> lipid phases induced by protein-lipid interactions (Lehtonen and Kinnunen,<br />
1997; Dumas et al., 1997; Hinderliter et al, 2004).<br />
43