ArticleEnvironmental science and pollution research international2018
Interactions between tetrahydroisoindoline-1,3-dione derivatives and human serum albumin via multiple spectroscopy techniques.
Article in Environmental science and pollution research international, 2018. 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.
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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
4 citing papers in PubMed.
- Unusually High Affinity of the PLK Inhibitors RO3280 and GSK461364 to HSA and Its Possible Pharmacokinetic Implications.Molecular pharmaceutics · 2023Article
- Article
- Effects of carbendazim on catalase activity and related mechanism.Environmental science and pollution research international · 2020Article
- Interactions of Bromocarbazoles with Human Serum Albumin Using Spectroscopic Methods.Molecules (Basel, Switzerland) · 2018Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Some tetrahydroisoindoline-1,3-dione derivatives (TDDs) possess potent herbicidal activity. To assess possible impacts of TDDs on humans, the interactions between TDDs and human serum albumin (HSA) were evaluated with steady-state and time-resolved fluorescence spectroscopy, synchronous fluorescence spectroscopy, Fourier transform-infrared spectroscopy, and circular dichroism spectroscopy. The thermodynamic data obtained at temperatures of 298, 307, and 316 K indicate that TDDs spontaneously bind to HSA and thus form a TDD-HSA complex. The conformation and secondary structure of HSA are changed, and the intrinsic fluorescence of HSA is statically quenched by TDDs. Moreover, the TDD-HSA complex is formed primarily through electrostatic interactions and has only one binding site on HSA. A competitive ligand-binding assay revealed that site II (subdomain IIIA) displays the greatest affinity for TDDs. In addition, an acute toxicity bioassay showed no zebrafish mortality upon exposure to 4000 μg L
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