Journal
SPECTROSCOPY-BIOMEDICAL APPLICATIONS
Volume 25, Issue 2, Pages 113-122Publisher
IOS PRESS
DOI: 10.1155/2011/195489
Keywords
Binding mechanism; human serum albumin; thiacloprid; spectroscopic techniques; molecular modeling
Categories
Funding
- Nanometer Technology Special Project [1052NM06700]
- Shanghai Municipal Science and Technology Commission [08DZ0505000]
- Jiangsu Education Department [JHZD09-18]
Ask authors/readers for more resources
Fluorescence spectroscopy, UV absorption, circular dichroism (CD) spectroscopy and molecular modeling methods were used to characterize the binding properties of thiacloprid (TL) with human serum albumin (HSA) at molecular level under physiological conditions. The fluorescence intensity of HSA decreased regularly with the gradually increasing concentration of thiacloprid. The binding constant K at three different temperatures (290, 300 and 310 K) were 3.07, 2.74 and 1.35 x 104 M-1, respectively, for TL-HSA interaction have been calculated from the relevant fluorescence data. CD spectroscopic measurements have shown that the secondary structures of the protein have been changed by the interaction of thiacloprid with HSA. Furthermore, the study of molecular modeling indicated that thiacloprid could be located on the surface of the binding pocket of subdomains IIA in HSA. The hydrophobic interaction was the major acting force and there are H-bonds and electrostatic interactions between TL and HSA, which is in good agreement with the results from the experimental thermodynamic parameters (the enthalpy change Delta H-0 and the entropy change Delta S-0 were calculated to be - 20.378 kJ/mol and 16.328 J/mol K according to the Van't Hoff equation).
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available