Novel inhibitors of enkephalin-degrading enzymes. I: Inhibitors of enkephalinase by penicillins

J Enzyme Inhib. 1989;3(2):91-101. doi: 10.3109/14756368909030368.

Abstract

Several penicillins have been found to have pro-antinociceptive properties and also to be enkephalinase (neutral endopeptidase-24.11) inhibitors, carfecillin being the most potent. Carfecillin i.c.v. (but not i.p.) had significant antinociceptive activity in the mouse tail immersion test and completely suppressed abdominal constrictions (acetic acid) in mice (IC50 = 23 micrograms/animal). In combination with (D-Ala2-D-leu5)-enkephalin (DADL) i.c.v. in the abdominal constriction test the complete protection observed was reversed by the opioid receptor antagonist naltrexone. Carfecillin was a competitive inhibitor of enkephalinase from mouse brain striata (IC50 = 207 + 57 nM, cf thiorphan 10.6 +/- 1.9 nM) but did not inhibit other known enkephalin- degrading enzymes. Carfecillin provides a new lead structure for the development of more potent enkephalinase inhibitors.

MeSH terms

  • Analgesics*
  • Animals
  • Brain / enzymology
  • Enkephalin, Leucine-2-Alanine / pharmacology*
  • Isoenzymes / antagonists & inhibitors
  • Male
  • Mice
  • Mice, Inbred Strains
  • Naltrexone / pharmacology
  • Neprilysin / antagonists & inhibitors*
  • Pain / physiopathology*
  • Penicillins / pharmacology*
  • Thiorphan / pharmacology
  • Time Factors

Substances

  • Analgesics
  • Isoenzymes
  • Penicillins
  • Naltrexone
  • Enkephalin, Leucine-2-Alanine
  • Thiorphan
  • Neprilysin