439918-60-2Relevant academic research and scientific papers
Biological active analogues of the opioid peptide biphalin: Mixed α/β3-peptides
Mollica, Adriano,Pinnen, Francesco,Costante, Roberto,Locatelli, Marcello,Stefanucci, Azzurra,Pieretti, Stefano,Davis, Peg,Lai, Josephine,Rankin, David,Porreca, Frank,Hruby, Victor J.
supporting information, p. 3419 - 3423 (2013/06/05)
Natural residues of the dimeric opioid peptide Biphalin were replaced by the corresponding homo-β3 amino acids. The derivative 1 containing hβ3 Phe in place of Phe showed good μ- and δ-receptor affinities (Kiδ =
Endomorphin-1 analogues containing β-proline are μ-opioid receptor agonists and display enhanced enzymatic hydrolysis resistance
Cardillo, Giuliana,Gentilucci, Luca,Qasem, Ahmed R.,Sgarzi, Fabio,Spampinato, Santi
, p. 2571 - 2578 (2007/10/03)
In this paper we describe the synthesis and affinity toward the μ-opioid receptor of some tetrapeptides obtained from endomorphin-1, H-Tyr-Pro-Trp-Phe-NH2 (1), by substituting each amino acid in turn with its homologue. The ability to bind μ -opioid receptors depends on the β-amino acid, and in particular 4, which contains β-L-Pro, has a KI, in the nanomolar range. The peptides 4 and 5 are significantly more resistant to enzymatic hydrolysis than 1. The same compounds, as well as the μ-opioid receptor agonist DAMGO, produced a concentration-dependent inhibition of forskolin-stimulated cyclic AMP formation, thus behaving as μ-opioid agonists. These features suggest that this novel class of endomorphin-1 analogues may represent suitable candidates for the in vivo investigation as potential μ-opioid receptor agonists.
