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

Abstract

Quinoline yellow (QY), a synthetic colourant widely used in the food industry, has caused extensive concerns because of its potentially harmful effects on human health. In the present work, the interactions between QY and human serum albumin (HSA) were characterized by multiple spectroscopic methods, a chemometric algorithm, and molecular modelling studies. The concentration profiles and pure spectra obtained for the components (QY, HSA and QY-HSA complex) from analyses of the expanded UV-visible absorption data matrices by multivariate curve resolution alternating least squares confirmed the QY-HSA interaction process. QY quenched the fluorescence of HSA through formation of a QY-HSA complex that was stabilized by moderate affinity. Hydrophobic forces and hydrogen bonding play major roles in the binding of QY to HSA. Site-specific marker-induced displacement results suggest that QY binds to subdomain IIA of HSA. This was corroborated by the molecular docking results. Decreases in HSA surface hydrophobicity and free sulfhydryl group content indicate that QY causes a contraction of the peptide strand in HSA, hiding the hydrophobic patches of the protein. Analyses by UV-visible absorption, circular dichroism, and three-dimensional fluorescence spectroscopy found that QY causes microenvironmental perturbations around the fluorophores and secondary structure changes in HSA. 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.