Académique Documents
Professionnel Documents
Culture Documents
Review
Vol.xxx No.x
Institute for Medicine and Engineering, Departments of Physiology, Physics, Bioengineering, University of Pennsylvania,
Philadelphia, PA 19104, USA
2
Helsinki Biophysics & Biomembrane Group, Department of Medical Chemistry, Institute of Biomedicine, University of Helsinki,
FIN-00014 Helsinki, Finland
0962-8924/$ see front matter 2006 Elsevier Ltd. All rights reserved. doi:10.1016/j.tcb.2006.08.009
Please cite this article as: P.A. Janmey, P.K.J. Kinnunen, Biophysical properties of lipids and dynamic membranes, TRENDS in Cell Biology (2006), doi:10.1016/j.tcb.2006.08.009
TICB-382; No of Pages 9
Review
Figure I. The lipids found in the plasma membrane. Abbreviations: PI, phosphatidylinositol; PIP, phosphatidylinositol phosphate; PIP2, PtdIns(4,5)P2;
PIP3, phosphatidylinositol (3,4,5)-trisphosphate.
www.sciencedirect.com
Please cite this article as: P.A. Janmey, P.K.J. Kinnunen, Biophysical properties of lipids and dynamic membranes, TRENDS in Cell Biology (2006), doi:10.1016/j.tcb.2006.08.009
TICB-382; No of Pages 9
Review
Figure I. Structures formed by different lipids: (a) inverted conical lipids, such
as detergent molecules, lysophospholipids and polyphosphoinositides; (b)
cylindrical-shaped lipids, such as phosphatidylcholine and sphingomyelin; (c)
conical lipids, such as diacylglycerol and PE.
Vol.xxx No.x
www.sciencedirect.com
Please cite this article as: P.A. Janmey, P.K.J. Kinnunen, Biophysical properties of lipids and dynamic membranes, TRENDS in Cell Biology (2006), doi:10.1016/j.tcb.2006.08.009
TICB-382; No of Pages 9
Review
Line tension
When a heterogeneous population of membrane lipids separate into
domains, the border between domains results in lipid packing that
is different from that inside and outside the domain, resulting from
such effects as the differences in height between the domains. The
deformation of molecules at the domain boundary that occurs mainly
to prevent exposure of hydrophobic regions to water costs energy,
and this energy per length of the boundary is called the line tension.
The magnitude of the line tension, which is generally not measurable
directly, contributes to the parameters that determine domain size
and stability.
Lateral pressures
A pressure due to loss of chain entropy within the hydrophobic
domain creates compressive forces within the bilayer, the magnitude
of which depends on the distance into the center of the bilayer, the
nature of the hydrophobic chains (e.g. saturated, unsaturated, single
chains or sterols) and the membrane curvature.
A compression force acts at the hydrophilic interface to crowd the
headgroup close enough to minimize exposure of the hydrophobic
chains to water. These lateral forces are present even if no external
force is applied to the membrane. Because such forces resulting
from, for example, osmotic stress, membrane bending, or pulling on
transmembrane proteins deform the membrane, the lateral forces
are also affected and therefore the structure of proteins inserted in the
bilayer can change. See Figure II.
Figure II. (a) The forces that act within the bilayer. Black lines represent the
hydrophobic chains and blue dots the hydrophilic headgroup. (b) The
corresponding lateral pressure, p(z), at different distances (z) across the bilayer
thickness. Strong tensions at the interfaces are balanced by positive pressures
through the interior, which are greatest near the interfaces. When the areas
under the curves add to zero, the membrane is globally at rest. The red
arrows show how a mismatch in the thickness of a transmembrane protein and
the lipid bilayer acyl chains moves the regions of high pressure up or down
along the z-axis, and the blue arrows show how bending the membrane alters
the pressure gradient within the bilayer. Adapted from [39,69].
www.sciencedirect.com
Please cite this article as: P.A. Janmey, P.K.J. Kinnunen, Biophysical properties of lipids and dynamic membranes, TRENDS in Cell Biology (2006), doi:10.1016/j.tcb.2006.08.009
TICB-382; No of Pages 9
Review
An example of how interfacial forces contribute to channel function is provided by two recent theoretical models
that consider the changes in free energy as the spatial
relationship between a membrane channel and the membrane in which it is embedded changes. As shown in
Figure 2, a typical transmembrane channel, for example
a mechanosensitive ion channel such as a TRP channel,
has an asymmetric profile within the hydrophobic part of
the lipid bilayer, characterized by the angle u and a
hydrophobic height W that is less than the bilayer
Vol.xxx No.x
Figure 2. Cross section of a mechanosensitive transmembrane complex such as a channel in its closed configuration. The geometry of the protein is described by three
parameters: the radius R, of the folded polypeptide, the thickness W of its hydrophobic domain, and the angle u that the hydrophobic domain boundary makes with a line
perpendicular to the membrane surface. The hydrophobic mismatch, 2U, is the difference between the hydrophobic protein thickness, W, and the bilayer equilibrium
thickness, 2a. Changes in the lateral bilayer forces in each leaflet can alter the polypeptide structure embedded within, and tilting of the protein [42] or moving it up or down
[40] will subject it to a different force profile within the bilayer that can alter the folding of the polypeptide. Adapted from Ref. [43].
www.sciencedirect.com
Please cite this article as: P.A. Janmey, P.K.J. Kinnunen, Biophysical properties of lipids and dynamic membranes, TRENDS in Cell Biology (2006), doi:10.1016/j.tcb.2006.08.009
TICB-382; No of Pages 9
Review
www.sciencedirect.com
Please cite this article as: P.A. Janmey, P.K.J. Kinnunen, Biophysical properties of lipids and dynamic membranes, TRENDS in Cell Biology (2006), doi:10.1016/j.tcb.2006.08.009
TICB-382; No of Pages 9
Review
Vol.xxx No.x
www.sciencedirect.com
Please cite this article as: P.A. Janmey, P.K.J. Kinnunen, Biophysical properties of lipids and dynamic membranes, TRENDS in Cell Biology (2006), doi:10.1016/j.tcb.2006.08.009
TICB-382; No of Pages 9
Review
www.sciencedirect.com
Please cite this article as: P.A. Janmey, P.K.J. Kinnunen, Biophysical properties of lipids and dynamic membranes, TRENDS in Cell Biology (2006), doi:10.1016/j.tcb.2006.08.009
TICB-382; No of Pages 9
Review
Vol.xxx No.x
www.sciencedirect.com
Please cite this article as: P.A. Janmey, P.K.J. Kinnunen, Biophysical properties of lipids and dynamic membranes, TRENDS in Cell Biology (2006), doi:10.1016/j.tcb.2006.08.009