Synthesis and biological activity of carboxyl terminally extended dermorphins
| Autor: | Mauro Marastoni, Severo Salvadori, Giuliano Marzola, Ettore Ciro Degliuberti, Gianfranco Balboni, Roberto Tomatis |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
animal structures
integumentary system Stereochemistry Guinea Pigs Biological activity Dermorphin Pharmacology Biochemistry Structure-Activity Relationship chemistry.chemical_compound Subcutaneous injection Opioid Peptides Opioid chemistry embryonic structures Morphine medicine Peptide synthesis Animals Structure–activity relationship Amino Acid Sequence Opioid peptide Oligopeptides Muscle Contraction medicine.drug |
| Zdroj: | International Journal of Peptide and Protein Research. 28:274-281 |
| ISSN: | 0367-8377 |
| DOI: | 10.1111/j.1399-3011.1986.tb03256.x |
| Popis: | Dermorphinoyl(DMR)-glycine, DMR-sarcosine and DMR-glycyl-arginine have been prepared in order to examine the effect of C-terminal extension of dermorphin (H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-Ser-NH2) on opioid activity. On GPI preparation the addition of Gly, Sar, or Gly-Arg to the carboxyl terminus of dermorphinoic acid was detrimental to mu activity: dermorphinoyl-derivatives, in fact, retain only 5-20% of dermorphin potency. Following intracerebroventricular administration (tail-flick test), whereas the analgesic activities of compounds showed the trend dermorphin greater than DMR-Sar greater than DMR-Gly-Arg greater than DMR-Gly greater than morphine, the nonapeptide displayed highest activity after subcutaneous injection in mice: DMR-Gly-Arg was 2.5 and 10 times more potent than dermorphin and morphine, respectively. |
| Databáze: | OpenAIRE |
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