Opioid receptor selectivity of peptide models of β‐endorphin


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Two peptides, designed to contain structural models of the proposed hydrophilic linker domain (residues 6‐12) and amphiphilic α‐helical domain (residues 13‐29) in β‐endorphin, have been tested for their abilities to mimic the opioid receptor selectivity profile of the natural hormone. In competitive binding assays employing guinea‐pig brain membranes, both peptides displayed a much higher affinity for μ‐ and δ‐opioid receptors than for κ opioid receptors. Relative to β‐endorphin, the peptide models were 2‐3 times more potent in the μ and κ receptor binding assays, and about equipotent in the δ receptor binding assay. In guinea‐pig ileum assays, one peptide was equipotent to β‐endorphin and the other was twice as potent. Like β‐endorphin, their actions on this tissue were highly sensitive to naloxone antagonism, indicating that they were mediated by μ receptors and not κ receptors. In view of the design of the two peptide models, and their minimal homology to the natural hormone, these results provide additional evidence in support to our proposal for the functional conformation of β‐endorphin.

Original languageEnglish (US)
Pages (from-to)75-80
Number of pages6
JournalInternational Journal of Peptide and Protein Research
Issue number1
StatePublished - Jul 1989
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry


  • amphiphilic helix
  • opioid activity
  • peptide models
  • β‐endorphin

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