Next Article in Journal
A Cross-Sectional Study of the Association between Infant Hepatitis B Vaccine Exposure in Boys and the Risk of Adverse Effects as Measured by Receipt of Special Education Services
Next Article in Special Issue
Cocoa Farmers’ Compliance with Safety Precautions in Spraying Agrochemicals and Use of Personal Protective Equipment (PPE) in Cameroon
Previous Article in Journal
Residual Inequity: Assessing the Unintended Consequences of New York City’s Clean Heat Transition
Article Menu
Issue 1 (January) cover image

Export Article

Open AccessArticle
Int. J. Environ. Res. Public Health 2018, 15(1), 116; https://doi.org/10.3390/ijerph15010116

Biointeractions of Herbicide Atrazine with Human Serum Albumin: UV-Vis, Fluorescence and Circular Dichroism Approaches

Key Laboratory of Agri-Food Safety of Anhui Province, School of Resources and Environment, Anhui Agricultural University, Hefei 230036, China
*
Author to whom correspondence should be addressed.
Received: 22 December 2017 / Revised: 6 January 2018 / Accepted: 9 January 2018 / Published: 11 January 2018
(This article belongs to the Special Issue Occupational Pesticides Exposure)
Full-Text   |   PDF [4055 KB, uploaded 11 January 2018]   |  

Abstract

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. View Full-Text
Keywords: atrazine; fluorescence quenching; human serum albumin; spectroscopy atrazine; fluorescence quenching; human serum albumin; spectroscopy
Figures

Graphical abstract

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Zhu, M.; Wang, L.; Wang, Y.; Zhou, J.; Ding, J.; Li, W.; Xin, Y.; Fan, S.; Wang, Z.; Wang, Y. Biointeractions of Herbicide Atrazine with Human Serum Albumin: UV-Vis, Fluorescence and Circular Dichroism Approaches. Int. J. Environ. Res. Public Health 2018, 15, 116.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Environ. Res. Public Health EISSN 1660-4601 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top