Abstract
Mn 2+ binding to vesicles prepared from several different species of anionic phospholipids was determined as a function of temperature by electron paramagnetic resonance (EPR). The Mn 2+ affinities of phosphatidylserine, cardiolipin and egg yolk phosphatidylglycerol all increased monitonically with temperature. Vesicles prepared from hydrogenated and natural (bovine) phosphatidylserine were monitored with respect to hydrocarbon chain fluidity as well as Mn 2+ binding. Contrary to expectations based on surface potential considerations, the affinity of phosphatidylserine for divalent cations was apparently not lowered in going from the gel state to the liquid crystalline state of the bilayer. The results are instead consistent with an enhancement in cation affinity with increased lipid fluidity. Dipalmitoyl phosphatidylglycerol vesicle fluidity and Mn 2+ binding were also studied with EPR. A large reduction in the measured Mn 2+ affinity accompanied melting of the phospholipid, but observed hysteresis in the temperature dependence of the binding render uncertain any simple explanation based on changes in surface potential. Supplementary light scattering data indicated that vesicle aggregation was involved in the hysteresis phenomena.
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