ArticleBMC chemistry2019
Binding interaction of sodium benzoate food additive with bovine serum albumin: multi-spectroscopy and molecular docking studies.
Article in BMC chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 44 citations in OpenAlex.
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- Elastase inhibition by natural flavonoids: mechanistic insights and potential therapeutic applications.Frontiers in nutrition · 2025Article
- Binding interaction of sodium benzoate, potassium sorbate and sodium dihydrogen citrate with BSA as food preservatives: in Vitro analysis and computational studies.Scientific reports · 2024Article
- Novel thiazole-based cyanoacrylamide derivatives: DNA cleavage, DNA/BSA binding properties and their anticancer behaviour against colon and breast cancer cells.BMC chemistry · 2024Article
- In Vitro and In Vivo Functional Viability, and Biocompatibility Evaluation of Bovine Serum Albumin-Ingrained Microemulsion: A Model Based on Sesame Oil as the Payload for Developing an Efficient Drug Delivery Platform.Pharmaceuticals (Basel, Switzerland) · 2023Article
- Visible Light-Generated Antiviral Effect on Plasmonic Ag-TiOFrontiers in bioengineering and biotechnology · 2021Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sodium benzoate (SB) is widely used as a preservative in food industry, and bovine serum albumin (BSA) is a major carrier protein similar to human serum albumin (HSA), the study of the binding between the two has great significance on human health. In this paper, we systematically investigated the binding of SB and BSA under the simulated physiological conditions combining with various common analytical methods, e.g., fluorescence, UV-vis absorption, synchronous fluorescence and circular dichroism (CD) spectra, as well as molecular docking method. The fluorescence quenching measurements were respectively carried out at 298 K, 303 K and 308 K using the Stern-Volmer method. The results reveal that ground state SB-BSA complex was formed within the binding constants from 2.02 × 10
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