Article ID Journal Published Year Pages File Type
1234809 Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2009 7 Pages PDF
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 × 10−6 to 3.0 × 10−5 mol L−1. 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 ΔH0, the free energy change ΔG0 and the entropy change ΔS0 of 296 K were calculated to be −7.75, −27.68 kJ mol−1 and 67.33 J mol−1 K−1, respectively.
Related Topics
Physical Sciences and Engineering Chemistry Analytical Chemistry
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