Binding characteristics of a series of dimeric tripeptide enkephalins for δ opiate receptors in rat brain and NG108–15 cells
✍ Scribed by Yasuyuki Shimohigashi; Hiroaki Kodama; Tommaso Costa; Rudolf A. Lutz; Hao-Chia Chen; David Rodbard
- Publisher
- John Wiley and Sons
- Year
- 1989
- Tongue
- English
- Weight
- 500 KB
- Volume
- 2
- Category
- Article
- ISSN
- 0952-3499
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✦ Synopsis
The N-terminal tripeptide enkephalin analogue, Tyr-D-Ala-Gly, was dimerized at the C-terminus systematically with a series of a,w-diaminoalkanes, NH2-(CH,),-NH, (n = 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, and 22). The binding affinities of dimers for 6 opiate receptors in rat brain were evaluated and compared with those for 6 receptors in NGlO8-15 cells. Although the monomeric tripeptide amide was almost inactive, dimers showed a dramatic increase in binding affinity (8-900 times). The enhancement of affinity was apparently related to the number of methylene chains in the crosslinking spacer moiety, and it was maximal at n = 14-18 in the rat brain. In NG cells the activity increased progressively from n = 2 to n = 22 without reaching any apparent peak. These results suggest that 6 receptors in rat brain and NG cells may have slight structural differences.