Interaction between quinoline yellow and human serum albumin: spectroscopic, chemometric and molecular docking studies

Wang, Rui; Hu, Xiaofeng; Pan, Junhui; Gong, Deming; Zhang, Guowen

doi:10.1002/jsfa.9144

Cited by 16 publications

(4 citation statements)

References 40 publications

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“…After exposure to DHA‐S, the signal values of peak 1 and peak 2 are significantly reduced, indicating that DHA‐S destroyed the scattering effect of HSA, which is consistent with the RLS spectra result. Peak 3 mainly shows the spectral characteristics of Trp and Tyr residues 46 . After the reaction with DHS‐A, this peak was significantly reduced, indicating that DHS‐A quenched the fluorescence of HSA.…”

Section: Resultsmentioning

confidence: 99%

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Probing the potential toxicity by characterizing the binding mechanism of sodium dehydroacetate to human serum albumin

Cui

Xiao

et al. 2021

J Sci Food Agric

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BACKGROUND: Sodium dehydroacetate (DHA-S) is a common food additive, which can combine with serum proteins in the plasma, but the interaction mechanism between DHA-S and human serum albumin (HSA) is unclear. In this study, multiple spectroscopy techniques, isothermal titration calorimetry (ITC), molecular docking and esterase activity test were employed to investigate the interaction mechanism of DHA-S and HSA. RESULTS: A DHA-S-HSA complex was formed and the structure of HSA were altered by DHA-S. Since DHA-S changed the tight structure of the hydrophobic subdomain IIA where tryptophan (Trp) was placed, the hydrophobicity of the microenvironment of HSA was enhanced. With the addition of DHA-S, the skeleton structure of HSA became loose and the solvent shell on the HSA surface was destroyed. DHA-S altered the secondary structure of HSA, resulting in the decreased ⊍-helix and increased ⊎-sheet contents. The interaction was exothermic and spontaneous driven by van der Waals and hydrogen bonding. DHA-S inhibited the esterase activity of HSA. Molecular docking demonstrated that the binding site of DHA-S on HSA located at the cavity of subdomains IIA and IIIA, but the amino acids related to esterase activity of HSA were not in the binding pocket, indicating that the mechanism by which DHA-S inhibited HSA esterase activity was the change in protein structure.CONCLUSION: This study illustrated that DHA-S interacted with HSA and the structure and function of HSA were affected by DHA-S. This research could help to understand the toxicity of DHA-S and provide basic data for safe use of food additives.

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Section: Resultsmentioning

confidence: 99%

“…Peak 3 mainly shows the spectral characteristics of Trp and Tyr residues. 46 After the reaction with DHS-A, this peak was significantly reduced, indicating that DHS-A quenched the fluorescence of HSA. Peak 4 mainly reflects the information of the polypeptide backbone changes caused by the π-π* transition.…”

Section: Wileyonlinelibrarycom/jsfamentioning

confidence: 98%

Probing the potential toxicity by characterizing the binding mechanism of sodium dehydroacetate to human serum albumin

Cui

Xiao

et al. 2021

J Sci Food Agric

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“…The molecular docking technology is also used to explore the mechanisms of food dyes and HSA. The combination of quinoline yellow (QY) and HSA reduced the free sulfhydryl group content and surface hydrophobicity of the protein, and provided a new understanding for reducing the physiological toxicity of QY (Wang et al, 2019b). In addition, fragrant interaction occurred between Allura Red (AR) and Gln 196, while the formation of hydrogen bonding took place between AR and His 242 (Wu et al, 2015).…”

Section: Proteinmentioning

confidence: 99%

Recent developments in molecular docking technology applied in food science: a review

Tao

Huang

Wang

et al. 2019

Int J of Food Sci Tech

127

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Molecular docking is a theoretical simulation method based on bioinformatics, which studies the interaction between molecules (such as ligands and receptors), and predicts their binding modes and affinity via a computer platform. This technology acts as a promising mean in medicinal chemistry such as structurebased rational drug design, which is accepted by researchers in the scientific community. During recent years, various fundamental studies involving biomolecular interaction in the food matrix have gradually emerged. The remarkable advantages of molecular docking such as predicting experiments are attracting increasing attention for its application potential in various fields. This review presents the theory and software development of molecular docking, and emphasises its application in the field of food science, including nutritional components and food safety. Moreover, the operational mechanisms of molecular docking are further summarised in this review.

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“…Estos últimos se continúan usando dado que poseen tres características muy interesantes: producción muy barata, tinte muy fuerte y una buena estabilidad química (Downham y Collins, 2000;Oreopoulou et al, 2009). No obstante, los colorantes sintéticos, si bien son muy versátiles en la industria alimentaria se han hallado en varios estudios que presentan una correlación positiva entre el consumo de los mismos y diversas alteraciones en la salud como: la hiperactividad (Bateman et al, 2004;McCann et al, 2007;Oplatowska-Stachowiak y Elliott, 2015), los defectos en el ADN (Khan et al, 2020), las reacciones alérgicas dermatológicas (Bateman et al, 2004;Panachiyil et al, 2019), la interacción con proteínas (Basu Y Suresh Kumar, 2015; Shahabadi et al, 2017;Wang et al, 2019) (Wopara et al, 2021).…”

Section: Introductionunclassified

Caracterização De Corantes Para Elaboração De Cerejas Candeada: Eritrosina Versus Vermelho Gardenia

Pacheco¹,

Maldonado²,

Agüero³

et al. 2022

Agrárias: Pesquisa E Inovação Nas Ciências Que Alimentam O Mundo VIII

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O conteúdo deste livro está licenciado sob uma Licença de Atribuição Creative Commons Atribuição-Não-Comercial NãoDerivativos 4.0 Internacional (CC BY-NC-ND 4.0). Direitos para esta edição cedidos à Editora Artemis pelos autores. Permitido o download da obra e o compartilhamento, desde que sejam atribuídos créditos aos autores, e sem a possibilidade de alterá-la de nenhuma forma ou utilizá-la para fins comerciais.A responsabilidade pelo conteúdo dos artigos e seus dados, em sua forma, correção e confiabilidade é exclusiva dos autores. A Editora Artemis, em seu compromisso de manter e aperfeiçoar a qualidade e confiabilidade dos trabalhos que publica, conduz a avaliação cega pelos pares de todos manuscritos publicados, com base em critérios de neutralidade e imparcialidade acadêmica.

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Interaction between quinoline yellow and human serum albumin: spectroscopic, chemometric and molecular docking studies

Abstract: This work shows that QY binds to HSA, affecting its structural and functional properties, and provides new insights into the binding mechanism and a comprehensive understanding of the toxicity of QY to biological processes. © 2018 Society of Chemical Industry.

Cited by 16 publications

References 40 publications

Probing the potential toxicity by characterizing the binding mechanism of sodium dehydroacetate to human serum albumin

Probing the potential toxicity by characterizing the binding mechanism of sodium dehydroacetate to human serum albumin

Recent developments in molecular docking technology applied in food science: a review

Caracterização De Corantes Para Elaboração De Cerejas Candeada: Eritrosina Versus Vermelho Gardenia

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