129505-65-3Relevant academic research and scientific papers
Opioid peptides. Synthesis and biological properties of demorphin related hexapeptides
Salvadori,Marastoni,Balboni,Borea,Tomatis
, p. 171 - 177 (2007/10/02)
The Gly4 and/or Tyr5 residues in dermorphin hexapeptide (H-Tyr-D-Ala-Phe-Gly-Tyr-Pro-OH) were replaced by Nα-methyl- or D-amino acids in order to examine the effect on opioid activity. Two pseudopeptides (H-Tyr-D-Ala-Phe-Gly-ψ (NHCO)-Xaa-Pro-OH, Xaa - Tyr or Phe) in which the Gly4-Xaa bond is reversed, were also prepared. Metabolic stability, analgesia and selectivity of these compounds for different receptor populations have been investigated. Results suggest that the 12 new analogues showed a negligible affinity for the K binding site and some selectivity for μ- or δ receptors. In some cases the analgesic potencies seems to be related to enzymatic stability of the peptides.
