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Biophys J, May 1999, p. 2575-2586, Vol. 76, No. 5
Max-Planck-Institut für biophysikalische Chemie, Abteilung Spektroskopie, D-37070 Göttingen, Germany
Binding isotherms have been determined for the
association of horse heart cytochrome c with dioleoyl
phosphatidylglycerol (DOPG)/dioleoyl phosphatidylcholine (DOPC) bilayer
membranes over a range of lipid compositions and ionic strengths. In
the absence of protein, the DOPG and DOPC lipids mix nearly ideally.
The binding isotherms have been analyzed using double layer theory to
account for the electrostatics, either the Van der Waals or scaled
particle theory equation of state to describe the protein surface
distribution, and a statistical thermodynamic formulation consistent
with the mass-action law to describe the lipid distribution. Basic
parameters governing the electrostatics and intrinsic binding are
established from the binding to membranes composed of anionic lipid
(DOPG) alone. Both the Van der Waals and scaled particle equations of state can describe the effects of protein distribution on the DOPG
binding isotherms equally well, but with different values of the
maximum binding stoichiometry (13 lipids/protein for Van der Waals and
8 lipids/protein for scaled particle theory). With these parameters
set, it is then possible to derive the association constant,
Kr, of DOPG relative to DOPC for surface
association with bound cytochrome c by using the binding
isotherms obtained with the mixed lipid membranes. A value of
Kr (DOPG:DOPC) = 3.3-4.8, depending on the
lipid stoichiometry, is determined that consistently describes the
binding at different lipid compositions and different ionic strengths.
Using the value of Kr obtained it is possible to
derive the average in-plane lipid distribution and the enhancement in
protein binding induced by lipid redistribution using the statistical thermodynamic theory.
Biophys J, May 1999, p. 2575-2586, Vol. 76, No. 5
© 1999 by the Biophysical Society 0006-3495/99/05/2575/12 $2.00
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