Abstract
The affinities of certain endogenous opioid peptides and related sequences for μ, δ and k opiate receptors have been determined in membrane preparations from mouse brain. It was found that the KIs for the δ receptor changed very little when the sequence of the enkephalins was enlarged; on the contrary, the μ and especially the k activity were highly dependent not only on the specificity of the sequence but also on the length of the peptide. Most of the peptides have similar affinities for more than one receptor type. The enkephalins are the most selective for the δ receptor. β-Endorphin, BAM-12P, BAM-22P, peptide E and dynorphin A display the best potency at the μ site. Dynorphin A (1-8), dynorphin A and dynorphin B are the most selective for the k site.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 291-294 |
| Number of pages | 4 |
| Journal | Life Sciences |
| Volume | 33 |
| Issue number | SUPPL. 1 |
| DOIs | |
| State | Published - 1983 |
Bibliographical note
Funding Information:Javler Garz~n is a recipient of a NIH Fellowship, FO-5TW-03080. Pilar Sanchez-Blazquez is a recipient of a Fulbrlght-MEC Fellowship. N.M. Lee is the recipient of a NIDA Research Scientist Career Award. This work was supported by NIDA Grant DA-02643.
