Abstract
The affinity between sorafenib and human serum albumin (HSA) was investigated by molecular modeling techniques and spectroscopic methods. The results of fluorescence spectroscopy, three-dimensional (3D) fluorescence, Fourier transform infrared (FTIR) and circular dichroism (CD) spectroscopy suggest that sorafenib has a strong ability to quench the intrinsic fluorescence of HSA. The binding affinity (K A) and the number of binding sites (n) between sorafenib and HSA at 305 K were estimated as 2.64 × 104 L·mol−1 and 1, respectively. The apparent distance between the Trp214 and sorafenib is 4.41 nm. Additionally, the binding of sorafenib induced conformational changes of disulfide bridges of HSA with decrease of the α-helix content. The resonance light scattering (RLS) spectra showed that the dimension of the individual HSA molecules are larger after interaction with sorafenib. These studies provide more information on the potential pharmaceutical effects and toxicological risk assessment of sorafenib.
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