Biophysical study of phloretin with human serum albumin in liposomes using spectroscopic methods.

The ability of drugs to diffuse through the lipid bilayer of cell membranes is important for their metabolism, distribution, and efficacy. In this study, the interaction between phloretin and human serum albumin (HSA) in an L-egg lecithin phosphatidylcholine (PC) liposome suspension was investigated by fluorescence and absorbance spectroscopy. The spectroscopic and fluorescence quenching experiments show that phloretin molecules penetrated into the lumen of the liposome. The partition coefficient of phloretin in the PC liposome suspensions was calculated from fluorescence quenching measurements. The results show that phloretin efficiently quenches the intrinsic fluorescence of HSA through a combination of dynamic and static quenching. The values of Gibbs free energy, and the enthalpy and entropic change in the binding process of phloretin with HSA in the PC liposome suspensions were negative, suggesting that the binding process of phloretin and HSA was spontaneous. Hydrogen bonding and van der Waals force interactions play an important role in the interaction between the two molecules. In addition, binding of phloretin to HSA in liposome suspensions was investigated by synchronous fluorescence spectroscopy.