Binding characteristics of the novel highly selective delta agonist, [3H]IIe5,6deltorphin II

Following the description of the [3H]deltorphin II, it has been reported that the modification of deltorphin II with the substitution of Val5,6 residues by the more hydrophobic IIe5,6 residues leads to an increased affinity and selectivity. The IIe5,6 deltorphin II (Tyr-D-Ala-Phe-Gly-IIe-IIe-HH2) was tritiated by catalytic dehalogenation and labelled rat brain membrane sites with a Kd value of 0.40 nM and a Bmax of 121 fmol/mg protein. Competition binding experiments with various unlabelled subtype specific opioid receptor ligands resulted in mu/delta and kappa/delta selectivity ratios of 2400 and 18,000 respectively. Due to its high delta receptor affinity, delta selectivity and very low non-specific binding (< 20%), [3H]IIe5,6 deltorphin II, is a very useful tool for the identification and characterisation of delta opioid receptors.