For the first time, we have shown that a stereospecific interaction occurs between porcine pancreatic phospholipase A2 and a monomolecular film of amidophospholipid used as inhibitor. Direct binding experiments, using radiolabelled phospholipase A2, showed that 13 times more enzyme was bound to phospholipid films of the l series by comparison with films of the d series. These results were confirmed by indirect binding studies using re-spreading experiments. Kinetic studies of the porcine pancreatic PLA2, using enantiomeric acyl-amino phospholipid analogues, have shown that: (1) inhibitors of the l series are more potent than inhibitors of the d series, (2) inhibitors having a negative charge are more potent than zwitterionic inhibitors, (3) inhibitory power values are greater when evaluated in micellar system than in a the monolayer system, (4) the inhibitory power increases continuously with surface pressure. © 1992.
Ransac, S., Deveer, A. M. T. J., Rivière, C., Slotboom, A. J., Gancet, C., Verger, R., & De Haas, G. H. (1992). Competitive inhibition of lipolytic enzymes. V. A monolayer study using enantiomeric acylamino analogues of phospholipids as potent competitive inhibitors of porcine pancreatic phospholipase A2. Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism, 1123(1), 92–100. https://doi.org/10.1016/0005-2760(92)90175-U