Investigation on the Competition Interaction of Synthetic Food Colorants and Ciprofloxacin Hydrochloride with Bovine Serum Albumin by Fluorescence Spectroscopy

Abstract

The effects of synthetic food colorants like tartrazine (TTZ), sunset yellow (SY), and erythrosine (ETS) on the binding reaction between ciprofloxacin hydrochloride (CPFX) and bovine serum albumin (BSA) were investigated by fluorescence spectroscopy in the aqueous solution of pH = 7.40. Results showed that CPFX caused the fluorescence quenching of BSA through a static quenching procedure and the primary binding site was located at subdomain IIA of BSA (site I). According to the calculated thermodynamic parameters, it confirmed that CPFX bound to BSA by electrostatic interaction. In addition, the colorants affected the formation of BSA-CPFX complex. This resulted in an increase of the free, biological active fraction of CPFX. The binding distance of BSA-CPFX systems was evaluated according to Förster's theory. Results suggested that the binding distance were increased in the presence of synthetic food colorants.

Study on the interaction of food colourant quinoline yellow with bovine serum albumin by spectroscopic techniques

“…These results indicated that Qy interacted with the C@O and CAN groups in the protein polypeptides. Liu et al (2011) reported the interaction of synthetic food colourants like tartrazine (TTZ), sunset yellow (SY), and erythrosine (ETS) on the binding reaction with BSA-drug by fluorescence spectroscopy, and Bolel et al (2012) explained the binding of Cochineal Red A with two homologous serum albumins. Their results indicated that food colourants bound to BSA with a high affinity.…”

“…The effects of three synthetic food colourants on the ciprofloxacin hydrochloride -BSA complex were investigated (Liu, Yang, Xue, & Lu, 2011). Bolel et al, reported that the Cochineal Red A binding results in some conformational modification of serum albumins (Bolel et al (2012)).…”

Encapsulation of L‐dopa and catechol in bovine serum albumin nanocarrier using desolvation method and their in vitro release studies

“…The main difference, however, lies in the number of tryptophans (TRPs) with the BSA having two TRPs and the HSA with only one. [15] L-dopa with the molecular structure of L-3,-4-dihydroxyphenylalanine ( Figure 1a) is an amino acid as a part of normal biology of human, some animals as well as some species of plants. Some animals and humans produce it through the biosynthesis of amino acid, L-tyrosine.…”

Fluorescence Spectroscopy Study on the Interaction of Acetal Cleavable Anionic Surfactants and Bovine Serum Albumin

“…Protein is an integral part of life in organisms and can bind a wide variety of ligands such as surfactants, drugs, toxicants, and heavy metal ions [1][2][3][4][5][6]. Studies on the interactions between surfactants and proteins would be beneficial for understanding the occurence of surfactants acting as solubilizing or denaturing agents for proteins [7,8].…”