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  • Title: Increase in phospholipase A2 activity towards lipopolymer-containing liposomes.
    Author: Vermehren C, Kiebler T, Hylander I, Callisen TH, Jørgensen K.
    Journal: Biochim Biophys Acta; 1998 Aug 14; 1373(1):27-36. PubMed ID: 9733909.
    Abstract:
    Phospholipase A2 (PLA2)-catalyzed hydrolysis of dipalmitoylphosphatidylcholine (DPPC) liposomes incorporated with submicellar concentrations of polyethyleneoxide covalently attached to dipalmitoylphosphatidylethanolamine (DPPE-PEG2000) has been studied in the gel-to-fluid transition region of the host DPPC lipid bilayer matrix. By means of fluorescence and light-scattering measurements, the characteristic PLA2 lag time has been determined as a function of lipopolymer concentration and temperature. The degree of lipid hydrolysis was followed using radioactive labeled lipids. Differential scanning calorimetry has been applied to characterize the thermodynamic phase behavior of the lipopolymer-containing liposomes. A remarkable lipopolymer concentration-dependent decrease in the lag time was observed over broad temperature ranges. The radioactive measurements demonstrate an increase in catalytic activity for increasing amounts of lipopolymers in the bilayer. Hence, the lipopolymers act as a promoter of PLA2 lipid hydrolysis resulting in a degradation of the bilayer structure and a concomitant destabilization of the liposomes. This behavior is in contrast to the generally observed protective and stabilization effect in biological fluids exerted by lipopolymers in polymer-grafted liposomes. It is proposed that the enhanced activity of the small water soluble and interfacially active enzyme may involve a non-uniform distribution of the lipopolymers in the lipid matrix due to a coupling between local lipid bilayer curvature and composition of the non-bilayer-preferring lipopolymers.
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