Estimation of the Phospholipase A2 Selectivity on POPC/POPG Membranes Using the Interaction Map

Abstract The regulation of the activity and selectivity phospholipase A2 (PLA2), which is capable cleaving fatty acid in second position ( sn-2 ) phospholipid, carried out through membrane-binding catalytic sites enzyme. For hydrolytic activity, PLA2 must first bind to phospholipid membrane, binding efficiency depends on composition membrane. site formed by several tens amino acids its differs from enzyme enzyme; hydrophobic positively charged play a key role interaction. In this work, we investigated interaction bee venom with bilayers palmitoyl oleoylphosphatidylcholine (POPC) containing different amounts palmitoyloleoylphosphatidylglycerol (POPG). On basis measurements protein intrinsic fluorescence anisotropy lipid probe propose construction lipid–protein maps, reflect both changes structure These cause alterations label, turn measure mobility environment fluorescent probe. Analysis maps showed that there relationship between efficiency: optimum membranes POPC/POPG mixture lies region highest mobility, not negative charge. This dependence complements existing understanding process recognition membrane surface selection lipids already bound proposed mapping method can be extended other membrane-active proteins.