Abstract
Opioid receptor analyses of deltorphin A (H-Tyr- d-Met-Phe-His-Leu-Met-Asp-NH 2) analogues indicated the following: (a) increased negativity differentially affected affinities ( K i ) and selectivity ( K i μ/K i δ ); (b) shifted sequence heptapeptides, [Asp 5,Leu 6,Met-NH 2 7] and [Asp 4,His 5,Leu 6,Met-NH 2 7], reversed selectivity (δ → μ); (c) substitutions at positions 4, 5, and 6 diminished selectivity, with changes in residue 5 being the most detrimental; (d) C- terminal deletions differentially effected K i . These are the first data to demonstrate a reversal of δ selectivity in heptapeptides containing a negative charge and indicate that modifications in affinity occur through changes in both anionic and hydrophobic properties of residues at specific positions in the peptide. Deltorphin analogues might also be applied to differentiate between opioid receptor subsites.
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