Academic
Publications
Synthesis, radiolabeling and receptor binding of [ 3H][(1 S,2 R)ACPC 2]endomorphin-2

Synthesis, radiolabeling and receptor binding of [ 3H][(1 S,2 R)ACPC 2]endomorphin-2,10.1016/j.peptides.2006.09.004,Peptides,Attila Keresztes,Géza Tót

Synthesis, radiolabeling and receptor binding of [ 3H][(1 S,2 R)ACPC 2]endomorphin-2   (Citations: 1)
BibTex | RIS | RefWorks Download
Previously, we have shown that substitution of Pro2 for cis-2-aminocyclopentanecarboxylic acid, ACPC in endomorphin-2 results in an analogue with greatly augmented proteolytic stability, high μ-opioid receptor affinity and selectivity. We now report the synthesis and biochemical characterization of [3H][(1S,2R)ACPC2]endomorphin-2 with a specific activity of 1.41TBq/mmol (38.17Ci/mmol). Specific binding of [3H][(1S,2R)ACPC2]endomorphin-2 was saturable and of high affinity with an equilibrium dissociation constant, Kd=1.80±0.21nM and receptor density, Bmax=345±27fmol×mgprotein−1 at 25°C in rat brain membranes. Similar affinity values were obtained in kinetic and displacement assays. Both Na+ and Gpp(NH)p decreased the affinity proving the agonist character of the radioligand. [3H][(1S,2R)ACPC2]endomorphin-2 retained the μ-specificity of the parent peptide. The new radioligand will be a useful tool to map the topographical requirements of μ-opioid peptide binding due to its high affinity, selectivity and enzymatic stability.
Journal: Peptides , vol. 27, no. 12, pp. 3315-3321, 2006
Cumulative Annual
View Publication
The following links allow you to view full publications. These links are maintained by other sources not affiliated with Microsoft Academic Search.
Sort by: