Abstract
The binding properties on alizarin to human serum albumin (HSA) have been studied for the first time using fluorescence spectroscopy in combination with UV-visible absorbance spectroscopy. The results showed that alizarin strongly quenched the intrinsic fluorescence of HSA through a static quenching procedure, and non-radiation energy transfer occurred within the molecules. The number of binding sites was 1, and the efficiency of Förster energy transfer provided a distance of 1.83 nm between tryptophan and alizarin binding site. ΔH(θ), ΔS(θ) and ΔG(θ) were obtained based on the quenching constants and thermodynamic theory (ΔH(θ) < 0, ΔS(θ) > 0 and ΔG(θ) < 0). These results indicated that hydrophobic and electrostatic interactions are the main binding forces in the alizarin-HSA system. In addition, the results obtained from synchronous fluorescence spectra and three-dimensional fluorescence spectra showed that the binding of alizarin with HSA could induce conformational changes in HSA.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have