Abstract:
:Three naturally occurring dermorphin-like peptides from the skin of the frog Phyllomedusa bicolor, the related carboxyl-terminal amides, and some substituted analogs were synthesized, their binding profiles to opioid receptors were determined, and their biological activities were studied in isolated organ preparations and intact animals. The opioid binding profile revealed a very high selectivity of these peptides for mu sites and suggested the existence of two receptor subtypes, of high and low affinity. The peptides tested acted as potent mu opioid agonists on isolated organ preparations. They were several times more active in inhibiting electrically evoked contractions in guinea pig ileum than in mouse vas deferens. When injected into the lateral brain ventricle or peritoneum of rats, the high-affinity-site-preferring ligand, [Lys7-NH2]dermorphin, behaved as a potent analgesic agent. By contrast, the low-affinity-site-preferring ligand, [Trp4,Asn7-NH2]dermorphin, produced a weak antinociception but an intense catalepsy.
journal_name
Proc Natl Acad Sci U S Aauthors
Negri L,Erspamer GF,Severini C,Potenza RL,Melchiorri P,Erspamer Vdoi
10.1073/pnas.89.15.7203keywords:
subject
Has Abstractpub_date
1992-08-01 00:00:00pages
7203-7issue
15eissn
0027-8424issn
1091-6490journal_volume
89pub_type
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