E3S Web Conf.
Volume 245, 20212021 5th International Conference on Advances in Energy, Environment and Chemical Science (AEECS 2021)
|Number of page(s)||8|
|Section||Chemical Performance Research and Chemical Industry Technology Research and Development|
|Published online||24 March 2021|
Probing the interaction mechanism between Direct Red 80 and Human serum albumin: studies at the molecular level
1. School of Water Conservancy and Environment, University of Jinan, Jinan, Shandong Province, 250022
2. Water Resources Research Institute of Shandong Province, Jinan, 250014, China
* The corresponding author. Email: email@example.com
In recent years, azo dyes have received increasing attention due to their adverse effects on the environment and consumer health. However, the interaction mechanism between human serum albumin (HSA) and Direct Red 80 (DR80) is still unknown. The results showed that DR80 changed the secondary structure of HSA and made HSA skeleton loose and stretch. In addition, DR80 quenched the endogenous fluorescence of HSA by static quenching and changed the microenvironment of Trp in form of the hydrophobicity increased and the polarity decreased. Molecular docking results indicated that DR80 bound to the interface of three α-helical domains of HSA, hence, the changes in HSA structure and conformation was the main reason for the decline of its esterase activity. This work was done to illuminate the binding mechanism of DR80 and HSA, and to provide a different way for screening the low toxic dye at the molecular level.
© The Authors, published by EDP Sciences, 2021
This is an Open Access article distributed under the terms of the Creative Commons Attribution License 4.0, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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