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Biophys J, October 2000, p. 1747-1760, Vol. 79, No. 4
and
*Institut für Biochemie und Biophysik,
Friedrich-Schiller-Universität Jena, Philosophenweg 12, 07743 Jena, Germany, and Department of Physical Chemistry and
the Fritz Haber Research Center, The Hebrew University, Jerusalem
91904, Israel
The adsorption free energy of charged proteins on mixed
membranes, containing varying amounts of (oppositely) charged lipids, is calculated based on a mean-field free energy expression that accounts explicitly for the ability of the lipids to demix locally, and
for lateral interactions between the adsorbed proteins. Minimization of
this free energy functional yields the familiar nonlinear
Poisson-Boltzmann equation and the boundary condition at the membrane
surface that allows for lipid charge rearrangement. These two
self-consistent equations are solved simultaneously. The proteins are
modeled as uniformly charged spheres and the (bare) membrane as an
ideal two-dimensional binary mixture of charged and neutral lipids. Substantial variations in the lipid charge density profiles are found
when highly charged proteins adsorb on weakly charged membranes; the
lipids, at a certain demixing entropy penalty, adjust their concentration in the vicinity of the adsorbed protein to achieve optimal charge matching. Lateral repulsive interactions between the
adsorbed proteins affect the lipid modulation profile and, at high
densities, result in substantial lowering of the binding energy.
Adsorption isotherms demonstrating the importance of lipid mobility and
protein-protein interactions are calculated using an adsorption
equation with a coverage-dependent binding constant. Typically, at
bulk-surface equilibrium (i.e., when the membrane surface is
"saturated" by adsorbed proteins), the membrane charges are
"overcompensated" by the protein charges, because only about half
of the protein charges (those on the hemispheres facing the membrane)
are involved in charge neutralization. Finally, it is argued that the
formation of lipid-protein domains may be enhanced by electrostatic
adsorption of proteins, but its origin (e.g., elastic deformations
associated with lipid demixing) is not purely electrostatic.
Biophys J, October 2000, p. 1747-1760, Vol. 79, No. 4
© 2000 by the Biophysical Society 0006-3495/00/10/1747/14 $2.00
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