Journal
INTERNATIONAL JOURNAL OF ENVIRONMENTAL RESEARCH AND PUBLIC HEALTH
Volume 15, Issue 1, Pages -Publisher
MDPI
DOI: 10.3390/ijerph15010116
Keywords
atrazine; fluorescence quenching; human serum albumin; spectroscopy
Funding
- National Natural Science Foundation of China [31601657, 31701808]
- Anhui Agricultural University Youth Fund Project [2014zr003, yj2015-25]
- Provincial Training Programs of Innovation and Entrepreneurship for Undergraduates [201610364024]
- special funds of agro-product quality safety risk assessment of the Ministry of Agriculture of the People's Republic of China [GJFP201600501, GJFP201700501, GJFP201800501]
- Key Laboratory of Agri-food Safety of Anhui Province
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The herbicide atrazine is widely used across the globe, which is a great concern. To investigate its potential toxicity in the human body, human serum albumin (HSA) was selected as a model protein. The interaction between atrazine and HSA was investigated using steady-state fluorescence spectroscopy, synchronous fluorescence spectroscopy, UV-Vis spectroscopy, three-dimensional (3D) fluorescence spectroscopy and circular dichroism (CD) spectroscopy. The intrinsic fluorescence of HSA was quenched by the atrazine through a static quenching mechanism. Fluorescence spectra at two excitation wavelengths (280 and 295 nm) showed that the fluorescence quenched in HSA was mainly contributed to by tryptophan residues. In addition, the atrazine bound to HSA, which induced changes in the conformation and secondary structure of HSA and caused an energy transfer. Thermodynamic parameters revealed that this binding is spontaneous. Moreover, electrostatic interactions play a major role in the combination of atrazine and HSA. One atrazine molecule can only bind to one HSA molecule to form a complex, and the atrazine molecule is bound at site II (subdomain IIIA) of HSA. This study furthers the understanding of the potential effects posed by atrazine on humans at the molecular level.
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