SPECIFICITY OF ANTI-MORPHINE AND ANTI-MEPERIDINE ANTIBODIES AND THEIR REACTIVITY WITH OPIOID PEPTIDES

  • 1 January 1979
    • journal article
    • research article
    • Vol. 208  (3) , 498-506
Abstract
The specificity of antimorphine and antimeperidine antisera was measured by competitive displacement of immunizing radiolabeled haptens. Antimorphine antisera showed a high degree of specificity for a conformation of the phenylpiperidine moiety contained within the structures of morphine and its congeners of the morphinan and benzomorphan series. Antimeperidine antisera showed a high degree of specificity for a different conformation of the phenylpiperidine moiety represented within the structures of meperidine and its semisynthetic derivatives. The reactivity of methionine- and leucine-enkephalin, several synthetic enkephalin analogs and .alpha.- and .beta.-endorphin with the antibodies was tested using purified immunoglobulin G in order to avoid serum-induced proteolysis. No significant cross-reactivity of antimorphine antibodies with any opioid peptide was detected. All opioid peptides tested showed weak but immunologically specific cross-reactivity with antimeperidine antibodies. Apparently conformations analogous to the phenylpiperidine moiety in morphine as were proposed for [Tyr1] in opioid peptides do not appear to be present as measured by immunochemical methods. A conformation with weak stereochemical similarity to the phenylpeperidine moiety in meperidine dogs appear to be present. The possible homologies between [Phe4] of opiod peptides, meperidine and hydrophobic side chains of certain oripavine derivatives were discussed.