Abstract
The influence of electrostatic charges and non-electrostatic components on the adsorption of an aspartyl protease to lipid membranes was determined by measuring the zeta and the monolayer potentials of phosphatidylcholine and phosphatidylcholine-stearylamine membranes with and without cholesterol and correlated with the aggregation of liposomes. A significant change in zeta potential was found in lipid bilayers with net charges, which was affected by cholesterol. This adsorption also affected the dipole potential of monolayers with a similar composition, but in this case, it was not dependent on cholesterol. The reduction of the electrostatic and the dipole potential barrier caused an increase in the aggregation of liposomes covered by the protein, and this was dependent on the saturation level of the phospholipid hydrocarbon chains.
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