Journal
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
Volume 36, Issue 6, Pages 1490-1510Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2017.1329096
Keywords
Diazinon; human serum albumin; protein binding; ligand-protein interactions; organophosphorus herbicide
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Funding
- Kermanshah University of Medical Sciences [93487]
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In the present research, the binding properties of diazinon (DZN), as an organophosphorus herbicide, to human serum albumin (HSA) were investigated using combination of spectroscopic, electrochemistry, and molecular modeling techniques. Changes in the UV-Vis and FT-IR spectra were observed upon ligand binding along with a significant degree of tryptophan fluorescence quenching on complex formation. The obtained results from spectroscopic and electrochemistry experiments along with the computational studies suggest that DZN binds to residues located in subdomains IIA of HSA with binding constant about 1410.9M(-1)at 300K. From the thermodynamic parameters calculated according to the van't Hoff equation, the enthalpy change H degrees and entropy change S degrees were found to be -16.695 and 0.116 KJ/molK, respectively. The primary binding pattern is determined by hydrophobic interaction and hydrogen binding occurring in so-called site I of HSA. DZN could slightly alter the secondary structure of HSA. All of experimental results are supported by computational techniques such as docking and molecular dynamics simulation using a HSA crystal model.
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