Curious Results in the Prospective Binding Interactions of the Food Additive Tartrazine with ß-Lactoglobulin.

The detailed characterizations of the binding interactions between food additive tartrazine (TZ) and ß-lactoglobulin (ß-LG) have been investigated through spectroscopic techniques combined with a molecular modeling study. A series of analyses, such as hyperchromic change in the UV-visible spectra, temperature-dependent quenching constant, time-resolved fluorescence, and Rayleigh scattering measurements, show that quenching of ß-LG proceeds by a static quenching mechanism. TZ specifically binds with ß-LG in a stoichiometry ratio of 1:1, and the observed binding constants (104, K) are 7.64, 9.13, 9.72, and 10.79 at 293, 298, 303, and 308 K, respectively. However, the curious results of binding constants (K) with temperature, encountered in the static quenching, have been well explained on the basis of Le Chatelier's principle. Thermodynamic data and pH-dependent studies along with the surface hydrophobicity binding displacement assay reveal that the durable mode of binding is chiefly entropy-driven, revealing noteworthy interactions of such ionic molecules with the hydrophobic part of ß-LG. The modulation of protein conformation has been investigated through steady-state absorption spectroscopy, synchronous emission spectroscopy, circular dichroism, and dynamic light scattering studies. TZ acts as a potential inhibitor in fibrillogenesis. Furthermore, the molecular docking study offers accurate insights about the binding of TZ with ß-LG, in consistence with the experimental results. This study would be helpful in pharmaceutical, food, and industrial engineering chemistry research.

Characterization of domain-specific interaction of synthesized dye with serum proteins by spectroscopic and docking approaches along with determination of in vitro cytotoxicity and antiviral activity.

The interaction between a synthesized dye with proteins, bovine, and human serum albumin (BSA, HSA, respectively) under physiological conditions has been characterized in detail, by means of steady-state and time-resolved fluorescence, UV-vis absorption, and circular dichroism (CD) techniques. An extensive time-resolved fluorescence spectroscopic characterization of the quenching process has been undertaken in conjugation with temperature-dependent fluorescence quenching studies to divulge the actual quenching mechanism. From the thermodynamic observations, it is clear that the binding process is a spontaneous molecular interaction, in which van der Waals and hydrogen bonding interactions play the major roles. The UV-vis absorption and CD results confirm that the dye can induce conformational and micro-environmental changes of both the proteins. In addition, the dye binding provokes the functionality of the native proteins in terms of esterase-like activity. The average binding distance (r) between proteins and dye has been calculated using FRET. Cytotoxicity and antiviral effects of the dye have been found using Vero cell and HSV-1F virus by performing MTT assay. The AutoDock-based docking simulation reveals the probable binding location of dye within the sub-domain IIA of HSA and IB of BSA.