ArticleJournal of food and drug analysis2014
Binding interactions of niclosamide with serum proteins.
Article in Journal of food and drug analysis, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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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Who cites it
5 citing papers in PubMed, 39 citations in OpenAlex.
- Efficient Expression in the Prokaryotic Host System, Purification and Structural Analyses of the Recombinant Human ACE2 Catalytic Subunit as a Hybrid Protein with the B Subunit of Cholera Toxin (CTB-ACE2).The protein journal · 2024Article
- Article
- Novel Combined Preparation and Investigation of Bergenin-Loaded Albumin Nanoparticles for the Treatment of Acute Lung Injury: In Vitro and In Vivo Evaluations.Inflammation · 2022Article
- Interaction Behavior Between Niclosamide and Pepsin Determined by Spectroscopic and Docking Methods.Journal of fluorescence · 2015Article
- Interaction of gallic acid with trypsin analyzed by spectroscopy.Journal of food and drug analysis · 2015Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A study of the binding of niclosamide (NC) to serum proteins such as human serum albumin, hemoglobin, and globulin was carried out using fluorescence and UV-visible spectroscopy. Interactions between NC and these proteins were estimated by Stern-Volmer and van't Hoff equations. The binding constants and the thermodynamic parameters, ΔH, ΔS, and ΔG at different temperatures were also determined by using these equations. Data showed that NC may exhibit a static quenching mechanism with all proteins. The thermodynamic parameters were calculated. Data showed that van der Waals interactions and hydrogen bonds are the main forces for human serum albumin and hemoglobin. Globulin, however, bound to NC via hydrophobic interaction. The spectral changes of synchronous fluorescence suggested that both the microenvironment of NC and the conformation of the proteins changed in relation to their concentrations during NC's binding.
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Registered trials
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