Characterizing the Interaction between Tartrazine and Two Serum Albumins by a Hybrid Spectroscopic Approach

Abstract

Tartrazine is an artificial azo dye commonly used in food products. The present study evaluated the interaction of tartrazine with two serum albumins (SAs), human serum albumin (HSA) and bovine serum albumin (BSA), under physiological conditions by means of fluorescence, three-dimensional fluorescence, UV-vis absorption, and circular dichroism (CD) techniques. The fluorescence data showed that tartrazine could bind to the two SAs to form a complex. The binding process was a spontaneous molecular interaction procedure, in which van der Waals and hydrogen bond interactions played a major role. Additionally, as shown by the UV-vis absorption, three-dimensional fluorescence, and CD results, tartrazine could lead to conformational and some microenvironmental changes of both SAs, which may affect the physiological functions of SAs. The work provides important insight into the mechanism of toxicity of tartrazine in vivo.

Toxicological and safety assessment of tartrazine as a synthetic food additive on health biomarkers: A review

“…This provides a significant understanding on the mechanism of tartrazine toxicity in vivo (Pan et al, 2011). The synchronous fluorescence investigation indicated that tartrazine binds with the hemoglobin central cavity, which was confirmed by a molecular demonstrating study (Li et al, 2014).…”

Interaction of ergosterol with bovine serum albumin and human serum albumin by spectroscopic analysis

“…So, SAs are employed as models for investigating the interactions between ligands and proteins in vitro. Among albumins, bovine serum albumin (BSA) and human serum albumin (HSA) have been studied extensively because of their similar folding and well-known primary structure [2]. BSA shows 76 % similarity with that of HSA [3], which has a single-chain with 582 amino acid residues.…”

Interaction of oridonin with human serum albumin by isothermal titration calorimetry and spectroscopic techniques

“…9). The results can be 420 explained that the interaction between oridonin and HSA leads 421 to the loosening and unfolding of the protein skeleton and 422 increases the hydrophobicity of the microenvironment of HSA [37]. 423 The absorption data were analyzed using the following equa-424 tion [38][39][40] to estimate the binding constant K A between HSA 425 and oridonin: [Oridonin] À1 for oridonin-HSA system at 298 K and pH 7.40.…”