Abstract
The effect of the incorporation of linear (perfluoroalkyl)alkanes (C m F 2 m+1 C n H 2 n+1 , F mH n) into liposomes made of DMPC or DPPC on the activity of porcine pancreatic phospholipase A 2 was investigated. A large decrease in enzyme activity and modifications of the kinetic profile, especially at and above the phospholipid's phase transition temperature, were observed; both depend on the relative lengths of the phospholipid's fatty acid chains and of the H n segment of the F mH n molecule. With DMPC H n must have a minimum of 10 carbon atoms to be effective, as in F6H10, F8H10 and F4H12; F8H8 had no significant hydrolysis-rate-reducing effect. With DPPC H n must have a minimum of 12 carbon atoms, as in F4H12, while F8H8, F6H10 and F8H10 were ineffective. The absence of effect when C 10H 22 or C 16H 34 was incorporated establishes that the fluorinated segment, although its length (from C 4 to C 8) is not crucial, is required to hinder hydrolysis by PLA 2, indicating that this segment plays an important role in structuring the liposomal membrane.
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