Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1234809 | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy | 2009 | 7 Pages |
Abstract
BAFP (2,6-bis[4-(4-amino-2-trifluoromethylphenoxy)benzoyl] pyridine), a synthesized polyimide compound, was exploited for the first time to analyze its interaction with human serum albumin (HSA) by molecular modeling, fluorescence and Fourier transform infrared attenuated total reflection spectroscopy (FTIR ATR) with drug concentrations of 3.3 Ã 10â6 to 3.0 Ã 10â5 mol Lâ1. Molecular docking was performed to reveal the possible binding mode. The results suggested that BAFP can strongly bind to human serum albumin (HSA) and the primary binding site of BAFP is located in site II of HSA, which is supported by the results from the competitive experiment. The binding constants for the interaction of BAFP with HSA have been evaluated from relevant fluorescence data at different temperatures (296, 303, 310 and 308 K). The alterations of the protein secondary structure in the presence of BAFP in aqueous solution were quantitatively calculated by the evidences from FTIR ATR spectroscopes. The binding process was exothermic and spontaneous, as indicated by the thermodynamic analyses, and the major part of the binding energy is hydrophobic interaction, which is also in good agreement with the results of molecule modeling study. The enthalpy change ÎH0, the free energy change ÎG0 and the entropy change ÎS0 of 296 K were calculated to be â7.75, â27.68 kJ molâ1 and 67.33 J molâ1 Kâ1, respectively.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Wen-ying He, Hui-juan Chen, Fen-ling Sheng, Xiao-jun Yao,