Exploring the Interaction of Tartrazine (Food Additive) Dye With Catalase Using Biophysical and Bioinformatics Tools.
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| Název: | Exploring the Interaction of Tartrazine (Food Additive) Dye With Catalase Using Biophysical and Bioinformatics Tools. |
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| Autoři: | Al-Twaijry N; Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia., Khan MS; Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia., Alenad A; Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia., Alokail MS; Department of Biochemistry, College of Science, King Saud University, Riyadh, Saudi Arabia., Arshad M; Dental Health Department, College of Applied Medical Sciences, King Saud University, Riyadh, Saudi Arabia., Al Kheraif AA; Dental Health Department, College of Applied Medical Sciences, King Saud University, Riyadh, Saudi Arabia. |
| Zdroj: | Luminescence : the journal of biological and chemical luminescence [Luminescence] 2025 Dec; Vol. 40 (12), pp. e70361. |
| Způsob vydávání: | Journal Article |
| Jazyk: | English |
| Informace o časopise: | Publisher: Wiley & Sons Country of Publication: England NLM ID: 100889025 Publication Model: Print Cited Medium: Internet ISSN: 1522-7243 (Electronic) Linking ISSN: 15227235 NLM ISO Abbreviation: Luminescence Subsets: MEDLINE |
| Imprint Name(s): | Original Publication: Chichester, Sussex, UK : Wiley & Sons, c1999- |
| Výrazy ze slovníku MeSH: | Tartrazine*/chemistry , Tartrazine*/metabolism , Catalase*/chemistry , Catalase*/metabolism , Computational Biology* , Food Coloring Agents*/chemistry , Food Additives*/chemistry , Food Additives*/metabolism, Molecular Docking Simulation ; Circular Dichroism ; Thermodynamics ; Spectrometry, Fluorescence ; Molecular Structure ; Spectrophotometry, Ultraviolet |
| Abstrakt: | Tartrazine (synthetic food dye) has been known to exert oxidative stress-related effects, yet its direct impact on antioxidant enzymes like catalase remains poorly understood. This study explores the interaction between tartrazine (synthetic dye) and catalase using various spectroscopic and in silico techniques. UV-visible as well as spectrofluorometric analysis revealed the formation of a catalase-tartrazine complex with a static mode of quenching. A moderate binding affinity ranging from 0.35 to 1.66 × 10 4 M -1 was calculated for the complex. Positive ΔH (23.72 kcal/mol) and ΔS (28.57-29.72 kcal/mol) with negative ΔG (-4.84 to -5.99 kcal/mol) suggest the binding process is endothermic and spontaneous, driven by a favorable entropy change. Circular dichroism (CD) indicates the percent α-helix in catalase decreased from 28.06% to 23.29% upon tartrazine binding, indicating some structural alterations. In turn, the catalase activity was decreased (60%) at a higher concentration (100 μM) of tartrazine. Molecular docking analysis identified several active site residues, including Met349, Gly352, Arg353, and Thr360, as key players in the binding process. Further, simulation studies demonstrated that the complex of tartrazine with catalase maintained stability in an aqueous environment. Our findings hinted that the use of additives should be cautious as they may compromise the antioxidant defense mechanisms critical to human health. (© 2025 John Wiley & Sons Ltd.) |
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| Grant Information: | ORFFT-2025-124-1 Ongoing Research Funding Program, King Saud University, Riyadh, Saudi Arabia |
| Contributed Indexing: | Keywords: catalase; interaction; molecular docking; molecular simulation; spectroscopy; tartrazine |
| Substance Nomenclature: | I753WB2F1M (Tartrazine) EC 1.11.1.6 (Catalase) 0 (Food Coloring Agents) 0 (Food Additives) |
| Entry Date(s): | Date Created: 20251201 Date Completed: 20251201 Latest Revision: 20251201 |
| Update Code: | 20251201 |
| DOI: | 10.1002/bio.70361 |
| PMID: | 41321114 |
| Databáze: | MEDLINE |
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Nájsť tento článok vo Web of Science | Abstrakt: | Tartrazine (synthetic food dye) has been known to exert oxidative stress-related effects, yet its direct impact on antioxidant enzymes like catalase remains poorly understood. This study explores the interaction between tartrazine (synthetic dye) and catalase using various spectroscopic and in silico techniques. UV-visible as well as spectrofluorometric analysis revealed the formation of a catalase-tartrazine complex with a static mode of quenching. A moderate binding affinity ranging from 0.35 to 1.66 × 10 <sup>4</sup> M <sup>-1</sup> was calculated for the complex. Positive ΔH (23.72 kcal/mol) and ΔS (28.57-29.72 kcal/mol) with negative ΔG (-4.84 to -5.99 kcal/mol) suggest the binding process is endothermic and spontaneous, driven by a favorable entropy change. Circular dichroism (CD) indicates the percent α-helix in catalase decreased from 28.06% to 23.29% upon tartrazine binding, indicating some structural alterations. In turn, the catalase activity was decreased (60%) at a higher concentration (100 μM) of tartrazine. Molecular docking analysis identified several active site residues, including Met349, Gly352, Arg353, and Thr360, as key players in the binding process. Further, simulation studies demonstrated that the complex of tartrazine with catalase maintained stability in an aqueous environment. Our findings hinted that the use of additives should be cautious as they may compromise the antioxidant defense mechanisms critical to human health.<br /> (© 2025 John Wiley & Sons Ltd.) |
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| ISSN: | 1522-7243 |
| DOI: | 10.1002/bio.70361 |