33900-27-5

Upstream product

• 65864-22-4 (S)-2-amino-3-phenylpropionamide hydrochloride 
• 13139-14-5 Boc-Trp-OH 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 47355-10-2 Nα-tert-butoxycarbonyl-1-formyl-L-tryptophan 
• 81092-89-9 L-phenylalanine amide trifluoroacetate 
• 88463-18-7 (S)-2-[(tert-butoxycarbonyl)amino]-3-phenylpropionamide 

Downstream Products

• 158276-61-0 2-amino-N-(1-amino-1-oxo-3-phenylpropan-2-yl)-3-(1H-indol-3-yl)propanamide 
• 189388-22-5 endomorphin 1 
• 637778-50-8 Boc-Pro-Trp-PheNH₂ 
• 351184-02-6 Boc-Tyr-Pro-Trp-PheNH₂ 

Relevant academic research and scientific papers

Stability against enzymatic hydrolysis of endomorphin-1 analogues containing β-proline

The enantiomer of endomorphin-1 (Tyr-Pro-Trp-PheNH2) and the analogues containing (S)-or (R)-β-proline have been synthesized, and their affinities towards μ-opioid receptors have been measured. As expected, the incubations of the different peptides with some commercially available enzymes showed that the presence of D-residues gave strong resistance towards digestion. The presence of β-proline alone is sufficient to confer good resistance against the hydrolysis of the biologically strategic Pro-Trp bond.

Functional profiling of p53-binding sites in Hdm2 and Hdmx using a genetic selection system

Upregulation of structurally homologous oncoproteins Hdm2 and Hdmx has been linked to the depletion or inactivation of their common regulation target the tumor suppressor p53 protein leading to the progression of cancer. The restoration of the p53 functio

Endomorphin-1 analogs with enhanced metabolic stability and systemic analgesic activity: Design, synthesis, and pharmacological characterization

We synthesized four new analogs of endomorphin-1 by systematic chemical modifications. To identify the best possible drug candidates for clinical pain management and to investigate the potential contribution of these alterations to the biological activity, their pharmacological properties were determined. All of the analogs showed significantly enhanced metabolic stability. The fact that centrally mediated analgesia following peripheral administration was observed with one of the analogs suggested the approach design undertaken here had validity in the development of endomorphin-1 as a successful opioid drug for the clinic.

Conformational analysis and mu-opioid receptor affinity of short peptides, endomorphin models in a low polarity solvent.

Peptide carbamates containing the sequence H-Pro-Trp-PheNH2 showed in CDCl3 restricted conformations stabilized by the presence of a gamma-turn. To test the reliability of the peptides as endomorphin conformational models, we measured the affinities for mu-receptors labelled with [3H]-DAMGO. In particular, Cbz-Pro-Trp-PheNH2 displayed a nanomolar affinity.

Endomorphin-1 analogues containing β-proline are μ-opioid receptor agonists and display enhanced enzymatic hydrolysis resistance

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.