{"title":"Binding of Sunset Yellow, a food coloring, to human carbonic anhydrase II: Structural and functional insights from a multi-spectroscopic study","authors":"Faezeh Hasrati , Sirous Ghobadi , Zohreh Shariati","doi":"10.1016/j.cbi.2025.111746","DOIUrl":null,"url":null,"abstract":"<div><div>The interaction of sunset yellow (SY), a widely used food coloring, with human carbonic anhydrase II (hCA II) was investigated using multiple spectroscopic techniques, including fluorescence, UV–Vis, and circular dichroism. The results showed that SY binds to hCA II, causing measurable changes in its enzymatic activity and structural properties. Fluorescence analyses indicated a quenching mechanism, while circular dichroism revealed alterations in secondary and tertiary structures. Moreover, SY binding affected the protein surface hydrophobicity index and its thermodynamic stability as well. Overall, these findings highlight that SY can modulate the structure and function of hCA II, providing insights with potential relevance to toxicology and enzymology.</div></div>","PeriodicalId":274,"journal":{"name":"Chemico-Biological Interactions","volume":"421 ","pages":"Article 111746"},"PeriodicalIF":5.4000,"publicationDate":"2025-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Chemico-Biological Interactions","FirstCategoryId":"3","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S000927972500376X","RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
The interaction of sunset yellow (SY), a widely used food coloring, with human carbonic anhydrase II (hCA II) was investigated using multiple spectroscopic techniques, including fluorescence, UV–Vis, and circular dichroism. The results showed that SY binds to hCA II, causing measurable changes in its enzymatic activity and structural properties. Fluorescence analyses indicated a quenching mechanism, while circular dichroism revealed alterations in secondary and tertiary structures. Moreover, SY binding affected the protein surface hydrophobicity index and its thermodynamic stability as well. Overall, these findings highlight that SY can modulate the structure and function of hCA II, providing insights with potential relevance to toxicology and enzymology.
期刊介绍:
Chemico-Biological Interactions publishes research reports and review articles that examine the molecular, cellular, and/or biochemical basis of toxicologically relevant outcomes. Special emphasis is placed on toxicological mechanisms associated with interactions between chemicals and biological systems. Outcomes may include all traditional endpoints caused by synthetic or naturally occurring chemicals, both in vivo and in vitro. Endpoints of interest include, but are not limited to carcinogenesis, mutagenesis, respiratory toxicology, neurotoxicology, reproductive and developmental toxicology, and immunotoxicology.