Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5398816 | Journal of Luminescence | 2015 | 34 Pages |
Abstract
The interaction of hepatitis B drug, adefovir dipivoxil with human serum albumin (HSA) was studied by using UV-vis, fluorometric, circular dichroism (CD) and molecular docking techniques. The results indicated that the binding of the drug to HSA caused fluorescence quenching through static quenching mechanism with binding constant of 1.3Ã103Â Mâ1. The thermodynamic parameters indicated that the hydrophobic force contacts are the major forces in the stability of protein-drug complex (ÎH>0 and ÎS>0). The displacement experiments using the site probes viz., warfarin and ibuprofen showed that adefovir dipivoxil could bind to the site III of HSA. The results of CD and UV-vis spectroscopy indicated that the binding of the drug induced some conformational changes in HSA. Furthermore, the study of molecular docking also confirmed binding of adefovir dipivoxil to the site III of HSA by hydrophobic interaction.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Physical and Theoretical Chemistry
Authors
Nahid Shahabadi, Monireh Falsafi, Saba Hadidi,