ArticleRSC advances2025
Deciphering the binding mechanism of tafamidis to calf thymus DNA: multimodal spectroscopic, thermodynamic, and computational perspectives.
Article in RSC advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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
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Who cites it
1 citing paper in PubMed.
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The interaction between small molecules and biological macromolecules is a crucial area of research with significant implications across various scientific disciplines. Tafamidis is a clinically approved drug for transthyretin-mediated amyloidosis, yet its molecular interactions with biological macromolecules such as DNA remain unexplored. Investigating such interactions is crucial for understanding its broader pharmacodynamic profile and potential off-target effects. In this study, the binding interaction between tafamidis and calf thymus DNA (ct-DNA) was investigated, for the first time, using a combination of spectroscopic techniques, viscosity measurements, ionic strength studies, thermodynamic analysis, and computational modeling. The key binding parameters, including the binding constant, number of binding sites, binding forces, and binding mode were determined. UV-vis spectroscopic analysis revealed a binding constant on the order of 10
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Registered trials
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