ArticleBiomolecules2024
Structural Studies on the Binding Mode of Bisphenols to PPARγ.
Article in Biomolecules, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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.
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Who cites it
4 citing papers in PubMed.
- Review
- Migration of Bisphenol A and Its Derivatives From Epoxy Coatings and Demand for BPA-NI Products: Scientific Insights and Perspectives Leading to Regulation (EU) 2024/3190.Chemistry, an Asian journal · 2025Review
- Endocrine disruptors, obesity, and metabolic syndrome.Turkish journal of medical sciences · 2025Review
- Molecular Thumbprints: Biological Signatures That Measure Loss of Identity.Biomolecules · 2024Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Bisphenol A (BPA) and bisphenol B (BPB) are widely used in the production of plastics, and their potential adverse health effects, particularly on endocrine disruption and metabolic health, have raised concern. Peroxisome proliferator-activated receptor gamma (PPARγ) plays a pivotal role in metabolic regulation and adipogenesis, making it a target of interest in understanding the development of obesity and associated health impacts. In this study, we employ X-ray crystallography and molecular dynamics (MD) simulations to study the interaction of PPARγ with BPA and BPB. Crystallographic structures reveal the binding of BPA and BPB to the ligand binding domain of PPARγ, next to C285, where binding of partial agonists as well as antagonists and inverse agonists of PPARγ signaling has been previously observed. However, no interaction of BPA and BPB with Y437 in the activation function 2 site is observed, showing that these ligands cannot stabilize the active conformation of helix 12 directly. Furthermore, free energy analyses of the MD simulations revealed that I341 has a large energetic contribution to the BPA and BPB binding modes characterized in this study.
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Registered trials
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