Binding and toxicological insights into Direct Yellow 8 and bovine serum albumin: fluorescence quenching and cytotoxicity studies
6 affiliations
- 1Nazionale delle Ricerche, Istituto Nazionale di Ottica (INO)
- 2School of Computational and Integrated Sciences, Jawaharlal Nehru University
- 3School of Biotechnology and Biomolecular Sciences, University of New South Wales
- 4Cancer Biology Laboratory, School of Life Sciences, Jawaharlal Nehru University
- 5Department of Electrical and Computer Engineering, University of Houston
- 6Laser Spectroscopy Laboratory, Department of Applied Physics, Delhi Technological University
Abstract
Industrial dyes are ubiquitous in nature, making it essential to assess their toxicological effects on humans and animals. Azo dyes, due to their structural composition (azo linkages), are resistant to biodegradation. Direct Yellow 8 (DY8), a monoazo industrial dye, may exhibit carcinogenic properties; therefore, it is imperative to extensively explore its effects on biomolecules. In this study, for the first time to the best of our knowledge, we elucidate the binding interaction between DY8 and bovine serum albumin (BSA) using multi spectroscopic techniques. Changes in the secondary structure of BSA were assessed using circular dichroism (CD). Fluorescence (FL) intensity of BSA was quenched upon interacting with DY8. Moreover, the lifetime of BSA is nearly constant in the presence of DY8. The change in the absorption spectrum, along with the constant FL lifetime in the presence of DY8, ensures the dominant static quenching. Molecular docking and dynamics simulations revealed a stable binding configuration with minimal fluctuation. Furthermore, the effect of DY8 in human embryonic kidney 293 (HEK 293) cells has also been discussed.
Related
- Frustration Quenching and Network Topology of the Energy Landscape as Primary Determinants of Protein-Ligand Binding Pose Prediction by Deep Learning Models
- Diene-Extended Chalcones Enable Red Fluorescence Detection of Human Serum Albumin Through FA1 Binding.
- Dynamic Protein Adduct Formation by Methylmercury: Molecular Targets, Ligand Exchange, and Toxicological Consequences
- AlvaQSAR: A Web-Based Platform for Molecular Prediction of Environmental and Toxicological Endpoints Aligned with OECD Principles
- Toxicological Exploration of Collagenase and Benzonase on Rat Precision-Cut Liver Slices.
BibTeX
@article{bisht2026binding,
title = {{Binding and toxicological insights into Direct Yellow 8 and bovine serum albumin: fluorescence quenching and cytotoxicity studies}},
author = {Babita Bisht and Sangeeta and Pinki Dey and Praveen K. Kujur and Avinash Kumar Singh and Mohan Singh Mehata},
journal = {Scientific Reports},
year = {2026},
month = sep,
doi = {10.1038/s41598-026-67669-6},
url = {https://doi.org/10.1038/s41598-026-67669-6},
note = {CC BY},
}
RIS
TY - JOUR
TI - Binding and toxicological insights into Direct Yellow 8 and bovine serum albumin: fluorescence quenching and cytotoxicity studies
AU - Babita Bisht
AU - Sangeeta
AU - Pinki Dey
AU - Praveen K. Kujur
AU - Avinash Kumar Singh
AU - Mohan Singh Mehata
PY - 2026
DA - 2026/09/01
JO - Scientific Reports
DO - 10.1038/s41598-026-67669-6
UR - https://doi.org/10.1038/s41598-026-67669-6
AB - Industrial dyes are ubiquitous in nature, making it essential to assess their toxicological effects on humans and animals. Azo dyes, due to their structural composition (azo linkages), are resistant to biodegradation. Direct Yellow 8 (DY8), a monoazo industrial dye, may exhibit carcinogenic properties; therefore, it is imperative to extensively explore its effects on biomolecules. In this study, for the first time to the best of our knowledge, we elucidate the binding interaction between DY8 and bovine serum albumin (BSA) using multi spectroscopic techniques. Changes in the secondary structure of BSA were assessed using circular dichroism (CD). Fluorescence (FL) intensity of BSA was quenched upon interacting with DY8. Moreover, the lifetime of BSA is nearly constant in the presence of DY8. The change in the absorption spectrum, along with the constant FL lifetime in the presence of DY8, ensures the dominant static quenching. Molecular docking and dynamics simulations revealed a stable binding configuration with minimal fluctuation. Furthermore, the effect of DY8 in human embryonic kidney 293 (HEK 293) cells has also been discussed.
SN - 2045-2322
ER -