Evidence map›Paper›PMID 39801251›Full record

ArticleArchiv der Pharmazie2025

The discovery of a new nonbile acid modulator of Takeda G protein-coupled receptor 5: An integrated computational approach.

Rudy Salam, Michael Bakker, Mária Krutáková, Alžbeta Štefela, Petr Pávek, Jurjen Duintjer Tebbens, Jan Zitko

Abstract read
In one paragraph

Article in Archiv der Pharmazie, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. ADMET & DMPK · 2026
    Review
  4. Article
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

7 authors.

Rudy SalamDepartment of Biophysics and Physical Chemistry, Faculty of Pharmacy, Charles University, Hradec Králové, Czech Republic.ORCID https://orcid.org/0009-0005-5879-5752
Michael BakkerDepartment of Biophysics and Physical Chemistry, Faculty of Pharmacy, Charles University, Hradec Králové, Czech Republic.ORCID http://orcid.org/0000-0002-4523-5570
Mária KrutákováDepartment of Pharmacology and Toxicology, Faculty of Pharmacy, Charles University, Hradec Králové, Czech Republic.
Alžbeta ŠtefelaDepartment of Pharmacology and Toxicology, Faculty of Pharmacy, Charles University, Hradec Králové, Czech Republic.ORCID https://orcid.org/0000-0003-1471-6248
Petr PávekDepartment of Pharmacology and Toxicology, Faculty of Pharmacy, Charles University, Hradec Králové, Czech Republic.ORCID https://orcid.org/0000-0001-8769-4196
Jurjen Duintjer TebbensDepartment of Biophysics and Physical Chemistry, Faculty of Pharmacy, Charles University, Hradec Králové, Czech Republic.ORCID https://orcid.org/0000-0003-0553-854X
Jan ZitkoDepartment of Pharmaceutical Chemistry and Pharmaceutical Analysis, Faculty of Pharmacy, Charles University, Hradec Králové, Czech Republic.ORCID https://orcid.org/0000-0003-0104-9925

Funding

Martina Roeselová Memorial Fellowship granted by the IOCB Tech FoundationMinistry of Education, Youth, and Sport of the Czech Republic 90140Ministry of Education, Youth, and Sport of the Czech Republic LM2018140Ministry of Education, Youth, and Sport of the Czech Republic SVV 260 663
6 · The paper itself

Abstract

The Takeda G protein-coupled receptor 5 (TGR5), also known as GPBAR1 (G protein-coupled bile acid receptor), is a membrane-type bile acid receptor that regulates blood glucose levels and energy expenditure. These essential functions make TGR5 a promising target for the treatment of type 2 diabetes and metabolic disorders. Currently, most research on developing TGR5 agonists focuses on modifying the structure of bile acids, which are the endogenous ligands of TGR5. However, TGR5 agonists with nonsteroidal structures have not been widely explored. This study aimed at discovering new TGR5 agonists using bile acid derivatives as a basis for a computational approach. We applied a combination of pharmacophore-based, molecular docking, and molecular dynamic (MD) simulation to identify potential compounds as new TGR5 agonists. Through pharmacophore screening and molecular docking, we identified 41 candidate compounds. From these, five candidates were selected based on criteria including pharmacophore features, a docking score of less than 9.2 kcal/mol, and similarity in essential interaction patterns with a reference ligand. Biological assays of the five hits confirmed that Hit-3 activates TGR5 similarly to the bile acid control. This was supported by MD simulation results, which indicated that a hydrogen bond interaction with Tyr240 is involved in TGR5 activation. Hit-3 (CSC089939231) represents a new nonsteroidal lead that can be further optimized to design potent TGR5 agonists.

Indexed as

Bile Acids and SaltsDrug DiscoveryReceptors, G-Protein-CoupledDose-Response Relationship, DrugHumansLigandsMolecular Docking SimulationMolecular Dynamics SimulationMolecular StructureStructure-Activity RelationshipBile Acids and SaltsGPBAR1 protein, humanLigandsReceptors, G-Protein-CoupledINT‐777molecular dockingnonbile acidpharmacophoreTGR5

Identifiers

PMID39801251
PMCPMC11726147

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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.