Evidence map›Paper›PMID 39432420›Full record

ArticleChemMedChem2025

Insights into Molecular Interactions and Biological Effect of Natural Stilbenoids at the TRPA1 Ion Channel.

Atefeh Saadabadi, Marja Rantanen, Parthiban Marimuthu, Ari-Pekka Koivisto, Patrik C Eklund, Outi M H Salo-Ahen

Abstract read
In one paragraph

Article in ChemMedChem, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Atefeh SaadabadiPharmaceutical Sciences Laboratory, Faculty of Science and Engineering, Åbo Akademi University, Tykistökatu 6, Turku, 20520, Finland.ORCID https://orcid.org/0000-0002-6115-1385
Marja RantanenPain Therapy Area, R&D, Orion Pharma, Tengströminkatu 8, Turku, 20360, Finland.
Parthiban MarimuthuPharmaceutical Sciences Laboratory, Faculty of Science and Engineering, Åbo Akademi University, Tykistökatu 6, Turku, 20520, Finland.ORCID https://orcid.org/0000-0003-4960-2160
Ari-Pekka KoivistoPain Therapy Area, R&D, Orion Pharma, Tengströminkatu 8, Turku, 20360, Finland.ORCID https://orcid.org/0000-0003-1389-9521
Patrik C EklundLaboratory of Molecular Science and Engineering, Faculty of Science and Engineering, Åbo Akademi University, Henrikinkatu 2, Turku, 20500, Finland.ORCID https://orcid.org/0000-0003-3040-5116
Outi M H Salo-AhenPharmaceutical Sciences Laboratory, Faculty of Science and Engineering, Åbo Akademi University, Tykistökatu 6, Turku, 20520, Finland.ORCID https://orcid.org/0000-0003-0725-126X

Funding

Finnish Cultural FoundationsMagnus Ehrnrooth FoundationSwedishTor, Joe and Pentti Borg Memorial Fund
6 · The paper itself

Abstract

Natural stilbenoids, polyphenolic compounds notably found in Scots pine and Norway spruce, have been shown to exhibit analgesic and anti-inflammatory effects through the TRPA1 channel, making them promising hits for the development of novel agents to treat inflammatory diseases and pain. In this study, we computationally investigated the putative binding sites of natural stilbenoids at the TRPA1 channel. Specifically, we employed molecular docking and MD simulation approaches to explore three known ligand binding sites at TRPA1. Furthermore, the biological effect of the studied compounds on TRPA1 was assessed in vitro using a fluorescent imaging plate reader (FLIPR™) calcium assay. Our modeling results suggest the stilbenoids exhibit higher affinity to the two agonist binding sites than the antagonistic site. Consistent with this, the in vitro results showed that the stilbenoids act as moderate TRPA1 channel agonists and likely inhibit the channel through a desensitization mechanism rather than act as pure TRPA1 antagonists. Additionally, our bias-force pulling simulations proposed an additional binding pocket for the natural stilbenoids that is distinct from the known ligand binding sites at TRPA1. The results of the study give useful insights into structure-based design and development of novel therapeutic TRPA1 modulators.

Indexed as

Biological ProductsNerve Tissue ProteinsStilbenesTransient Receptor Potential ChannelsTRPA1 Cation ChannelBinding SitesHumansMolecular Docking SimulationMolecular Dynamics SimulationMolecular StructureStructure-Activity RelationshipBiological ProductsNerve Tissue ProteinsStilbenesTransient Receptor Potential ChannelsTRPA1 Cation ChannelTRPA1 protein, humanIon channelsMolecular dockingMolecular dynamicsNatural stilbenoidsTRPA1 modulators

Identifiers

PMID39432420
PMCPMC11793850

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.