Opioid peptides. Structure-activity relationships in dermorphin tetrapeptides. I.
Characterisation and pharmacological data of twelve synthetic tetrapeptide analogs of dermorphin (opioid heptapeptide) are reported. An N-terminal tetrapeptide free acid or ester is less potent that the corresponding amide. Whereas substitution of Gly4 by another aminoacid residue is well tolerated, substitution of D-Ala2 by D- or L-alpha-aminoxypropionic acid causes a complete loss of activity. Finally, guanidination of the tetrapeptides results in an increase of peripheral and central opioid activity.
D000818:Animals; D001681:Biological Assay; D004723:Endorphins / Q000494:pharmacology*; D006168:Guinea Pigs; D007082:Ileum / Q000187:drug effects; D066298:In Vitro Techniques; D051379:Mice; D009842:Oligopeptides / Q000494:pharmacology*; D018847:Opioid Peptides; D013329:Structure-Activity Relationship
D004723:Endorphins; D009842:Oligopeptides; D018847:Opioid Peptides; C030058:dermorphin