| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1235841 | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy | 2012 | 7 Pages |
The interaction between bovine serum albumin (BSA) and the anticancer drug molecule ampelopsin (AMP) was investigated using fluorescence spectroscopy, circular dichroism (CD) spectra, and time-resolved spectra under simulated physiological conditions. Fluorescence data showed that the intrinsic fluorescence of BSA was strongly quenched by AMP in terms of a dynamic quenching process. Binding constants and binding sites were calculated. The thermodynamic parameters indicated that the hydrogen bonding and weak van der Waals force played a major role in the interaction. The site marker competitive experiments suggested that the binding site of AMP and BSA was probably located on site III. Based on the Förster's theory, the average binding distance between AMP and BSA was obtained (r = 5.47 nm). The binding of AMP and BSA leaded to conformational changes of BSA according to synchronous fluorescence spectra, CD data and mean fluorescence lifetime values.
Graphical abstractThe interaction between bovine serum albumin (BSA) and the anticancer drug ampelopsin (AMP) was investigated using fluorescence spectroscopy, circular dichroism (CD) spectra and time-resolved spectra under simulated physiological conditions. Efforts were made to investigate the quenching mechanism, binding constants, binding sites, binding mode, and the effects of AMP on the conformation of BSA.Figure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Binding behavior of AMP and BSA was investigated using fluorescence spectroscopy under simulated physiological conditions. ► Fluorescence spectra indicated that the quenching process was induced by dynamic quenching mechanism. ► The red shift of the maximum emission wavelength of BSA indicated that the tryptophan residues were gradually exposed to solvent owing to protein unfolding. ► Secondary structure parameters, obtained from CD spectra, of the AMP–BSA system indicated the unfolding of BSA. ► Time-resolved measurement indicated that the addition of AMP resulted in the deformation of the secondary structure of protein and hence the red shift of emission spectrum.
