| Autor: |
Katarzyna, Gach-Janczak, Justyna, Piekielna-Ciesielska, Anna, Adamska-Bartłomiejczyk, Karol, Wtorek, Federica, Ferrari, Girolamo, Calo', Agata, Szymaszkiewicz, Joanna, Piasecka-Zelga, Anna, Janecka |
| Rok vydání: |
2018 |
| Předmět: |
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| Zdroj: |
Peptides. 105 |
| ISSN: |
1873-5169 |
| Popis: |
Morphine and related drugs, which are the most effective analgesics for the relief of severe pain, act through activating opioid receptors. The endogenous ligands of these receptors are opioid peptides which cannot be used as antinociceptive agents due to their low bioactivity and stability in biological fluids. The major goal of opioid research is to understand the mechanism of action of opioid receptor agonists in order to improve therapeutic utility of opioids. Analgesic effects of morphine are mediated mostly through activation of the mu opioid receptor. However, in the search for safer and more effective drug candidates, analogs with mixed opioid receptor profile gained a lot of interest. Recently, the concept of biased agonists able to differentially activate GPCR downstream pathways, became a new approach in the design of novel drug candidates. It is hypothesized that compounds promoting G-protein signaling may produce analgesia while β-arrestin recruitment may be responsible for opioid side effects. In this report we showed that replacement of the tyrosine residue in the mu-selective ligand Tyr-c[d-Lys-Phe-Asp]NH |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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