Synthesis, conformation and opioid activity of deltorphins.
A series of deltorphin analogues was prepared by solid-phase peptide synthesis. Their opioid activity was evaluated in rat opiatic assay and their conformation was determined by two-dimension Nuclear Magnetic Resonance Spectroscopy. The analogues containing D-alanine acid at position 2 were much more potent in the assay than their corresponding isomers containing L-alanine acid at this position. The conformational analysis on NMR study in DMSO showed that C-terminal tetrapeptides of both deltorphin II and its L-alanine analog might form a 3(10) helix, which confirms that the substitution of D-amino acid at position 2 decreased the opioid activity.
Department of Biology, Lanzhou University, Gansu, China.
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Zhang
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D000700:Analgesics / Q000494:pharmacology*; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D004121:Dimethyl Sulfoxide; D007202:Indicators and Reagents; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008297:Male; D008958:Models, Molecular; D009842:Oligopeptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D010146:Pain / Q000503:physiopathology; D011487:Protein Conformation; D051381:Rats; D017208:Rats, Wistar; D016339:Spectrometry, Mass, Fast Atom Bombardment; D013329:Structure-Activity Relationship
D000700:Analgesics; D007202:Indicators and Reagents; D009842:Oligopeptides; C059567:deltorphin; D004121:Dimethyl Sulfoxide