Premium
Binding characteristics of a series of dimeric tripeptide enkephalins for δ opiate receptors in rat brain and NG108–15 cells
Author(s) -
Shimohigashi Yasuyuki,
Kodama Hiroaki,
Costa Tommaso,
Lutz Rudolf A.,
Chen HaoChia,
Rodbard David
Publication year - 1989
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.300020305
Subject(s) - tripeptide , opiate receptors , receptor , chemistry , opiate , stereochemistry , biochemistry , microbiology and biotechnology , medicine , biology , peptide , opioid , (+) naloxone
Abstract The N‐terminal tripeptide enkephalin analogue, Tyr‐ D ‐Ala‐Gly, was dimerized at the C‐terminus systematically with a series of α,ω‐diaminoalkanes, NH 2 (CH 2 ) n NH 2 ( n = 2, 4, 6, 8, 10, 12, 14, 16, 18, 20, and 22). The binding affinities of dimers for δ opiate receptors in rat brain were evaluated and compared with those for δ receptors in NG108–15 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 δ receptors in rat brain and NG cells may have slight structural differences.