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Experimental and computational studies on the binding of diazinon to human serum albumin
- Source :
- Journal of biomolecular structuredynamics. 36(6)
- Publication Year :
- 2017
-
Abstract
- 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 1410.9 M
- Subjects :
- 0301 basic medicine
030103 biophysics
Diazinon
Entropy
Serum albumin
Infrared spectroscopy
Serum Albumin, Human
Plasma protein binding
Molecular Dynamics Simulation
Fluorescence
Protein Structure, Secondary
03 medical and health sciences
chemistry.chemical_compound
Ultraviolet visible spectroscopy
Blood serum
Structural Biology
Spectroscopy, Fourier Transform Infrared
medicine
Humans
Molecular Biology
Chromatography
Binding Sites
biology
Circular Dichroism
Tryptophan
Hydrogen Bonding
General Medicine
Human serum albumin
body regions
Molecular Docking Simulation
030104 developmental biology
Spectrometry, Fluorescence
Biochemistry
chemistry
embryonic structures
biology.protein
Thermodynamics
Hydrophobic and Hydrophilic Interactions
medicine.drug
Protein Binding
Subjects
Details
- ISSN :
- 15380254
- Volume :
- 36
- Issue :
- 6
- Database :
- OpenAIRE
- Journal :
- Journal of biomolecular structuredynamics
- Accession number :
- edsair.doi.dedup.....df316511c9cdbda30b5504b9b7bb4baf