A novel opioid receptor site directed alkylating agent with irreversible narcotic antagonistic and reversible agonistic activities

Journal of Medicinal Chemistry
1980.0

Abstract

We now report on another line of evidence which provides additional support for the multiple modality or multiple receptor concept. Through use of the novel pair of receptor probes, 1 (β-FNA) and 2 (β-FOA), we present data which suggest that only 1 covalently binds to opioid receptors even though each of the compounds contains an identical alkylating moiety and forms a receptor complex. β-FNA (1) behaved as a potent reversible agonist with an IC50 of 4.8 × 10^-9 M when tested on the electrically stimulated guinea pig ileal longitudinal muscle preparation. The agonist effect of 1 could be reversed at all incubation times by washing or addition of naltrexone (7). However, when the ileum was incubated with 1 (2 × 10^-7 M) for different time periods and then washed (20X), a time-dependent, irreversible narcotic antagonistic effect against morphine was observed. The specificity of the blockage was suggested by the fact that the irreversible effects of 1 could be inhibited by prior addition of the reversible antagonist, naltrexone (7; 5 × 10^-6 M). Norepinephrine receptors were unaffected by β-FNA treatment. In view of the generally known chemical properties of Michael acceptors, the SH group is a good candidate for the nucleophile which forms a covalent bond with β-FNA (1). Significantly, when the ileum was treated with 2 (β-FOA) under conditions identical with those for 1, it produced a reversible agonistic effect (IC50 = 2.7 × 10^-8 M) but no agonism or morphine antagonism was observed following washing (20X) after 80 min of incubation. The agonistic effect of 2 also was blocked by the irreversible action of 1. Since the data suggest that 1 but not 2 forms a covalent bond with opioid receptors, it is likely that the receptor environments which interact with the fumaramate ester moiety of 1 and 2 are different. This indicates either that 1 and 2 interact differently with a single receptor or that they associate with different receptors, as proposed in the original concept.

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