ArticleACS medicinal chemistry letters2013
Structural and biological exploration of phe(3)-phe(4)-modified endomorphin-2 peptidomimetics.
Article in ACS medicinal chemistry letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
6 citing papers in PubMed.
- Trifluoromethylthio and Trifluoromethyl Functionalization of Endomorphin-1 Enhances its Hydrophobicity and Plasma Stability while Preserving its Affinity for the μ-Opioid Receptor.The Journal of organic chemistry · 2026Article
- Non-Canonical Amino Acids as Building Blocks for Peptidomimetics: Structure, Function, and Applications.Biomolecules · 2023Review
- Peptidomimetics and Their Applications for Opioid Peptide Drug Discovery.Biomolecules · 2022Review
- Synthesis, Pharmacological Evaluation, and Computational Studies of Cyclic Opioid Peptidomimetics Containing βMolecules (Basel, Switzerland) · 2021Article
- βMolecules (Basel, Switzerland) · 2020Article
- Synthesis and Pharmacology of α/β(3)-Peptides Based on the Melanocortin Agonist Ac-His-dPhe-Arg-Trp-NH2 Sequence.ACS medicinal chemistry letters · 2015Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This study reports on our ongoing investigation on hybrid EM-2 analogues, in which the great potential of β-amino acids was exploited to generate multiple conformational modifications at the key positions 3 and 4 of the parent peptide. The effect on the opioid binding affinity was evaluated, by means of ligand stimulated binding assays, which indicated a high nanomolar affinity toward the μ-receptor, with appreciable μ/δ selectivity, for some of the new compounds. The three-dimensional properties of the high affinity μ opioid receptor (MOR) ligands were investigated by proton nuclear magnetic resonance, molecular dynamics, and docking studies. In solution, the structures showed extended conformations, which are in agreement with the commonly accepted pharmacophore model for EM-2. From docking studies on an active form of the MOR model, different ligand-receptor interactions have been identified, thus confirming the ability of active compounds to assume a biologically active conformation.
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Registered trials
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