Molecular Alterations of Bovine Serum Albumin Induced by the Food Dye Acid Yellow 23: A Mechanistic Study
Year: 2026
Type: preprint
Abstract: The widespread use of synthetic food dyes, such as Acid Yellow 23 (AY 23), in the food, cosmetics, and pharmaceutical industries raises questions about their potential effects on biological systems and public health. The concentration-dependent interaction between AY 23 and bovine serum albumin (BSA), a crucial model protein for understanding pharmacokinetics and protein-ligand behaviour, was examined in this study. We demonstrate that, under physiological conditions, increasing the dye concentration from 50 µM to 200 µM leads to notable conformational changes, increased surface hydrophobicity, and protein aggregation, as determined using a multimodal biophysical approach including fluorescence spectroscopy. Direct visualisation verified these structural changes and aggregate formation, whereas hemolytic assay confirmed the high hemolytic nature of AY 23-induced fibrils. Additionally, this study provides a mechanistic basis for the toxicological effects of AY 23, underscoring the implications of food dyes for public health. Highlights Acid Yellow 23 (AY 23) modulates Bovine Serum Albumin (BSA) structure and leads to aggregation under physiological conditions. Structural alteration is followed by binding of AY 23 at the hydrophobic regions of BSA, causing perturbation of the protein. Confirmational changes induced by AY 23 in the BSA via interaction with Asp108, Pro110 and Ala193. Protein intermediates formed after AY 23 interaction are observed to be hemolytic in nature. Molecular mechanism of AY 23-mediated perturbation of BSA was assessed. Graphical Abstract
Institution: National Forensic Sciences University
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W7167840109