ArticleACS medicinal chemistry letters2015
Modulation of the Interaction between a Peptide Ligand and a G Protein-Coupled Receptor by Halogen Atoms.
Article in ACS medicinal chemistry letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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.
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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.
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Who cites it
7 citing papers in PubMed, 21 citations in OpenAlex.
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- 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
- Advances in 4-Hydroxycoumarin Chemistry: Functionalization, Prominent 4-Hydroxycoumarin-based Therapeutics and their Pharmacological Significance.Mini reviews in medicinal chemistry · 2026Review
- In vivo pharmacokinetic, pharmacodynamic and brain concentration comparison of fentanyl and para-fluorofentanyl in rats.Archives of toxicology · 2025Article
- Halogenation of Peptides and Proteins Using Engineered Tryptophan Halogenase Enzymes.Biomolecules · 2022Article
- Multifunctional Enkephalin Analogs with a New Biological Profile: MOR/DOR Agonism and KOR Antagonism.Biomedicines · 2021Article
- The Meta-Position of PheMolecules (Basel, Switzerland) · 2019Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Systematic halogenation of two native opioid peptides has shown that halogen atoms can modulate peptide-receptor interactions in different manners. First, halogens may produce a steric hindrance that reduces the binding of the peptide to the receptor. Second, chlorine, bromine, or iodine may improve peptide binding if their positive σ-hole forms a halogen bond interaction with negatively charged atoms of the protein. Lastly, the negative electrostatic potential of fluorine can interact with positively charged atoms of the protein to improve peptide binding.
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Registered trials
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