Competitive inhibition of lipolytic enzymes. V. A monolayer study using enantiomeric acylamino analogues of phospholipids as potent competitive inhibitors of porcine pancreatic phospholipase A2

  • Ransac S
  • Deveer A
  • Rivière C
 et al. 
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For the first time, we have shown that a stereospecific interaction occurs between porcine pancreatic phospholipase A2and 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.

Author-supplied keywords

  • (Porcine pancreas)
  • Inhibitor
  • Lipolytic enzyme
  • Monolayer
  • Phospholipase A2

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  • Stéphane Ransac

  • Annemieke M.T.J. Deveer

  • Claude Rivière

  • Arend J. Slotboom

  • Christian Gancet

  • Robert Verger

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