Fluorescence study on the interaction of human serum albumin with Butein in liposomes

Abstract

The interaction of Butein with human serum albumin in L-egg lecithin phosphatidycholine (PC) liposome has been investigated by fluorescence and absorption spectroscopy. The results of the fluorescence measurement indicated that Butein effectively quenched the intrinsic fluorescence of HSA via static quenching. The Stern Volmer plots in all the liposomesolutions showed a positive deviation fromthe linearity. According to the thermodynamic parameters, the hydrophobic interactions appeared be the major interaction forces between Butein and HSA. The effect of Butein on the conformation of HSA was also investigated by the synchronous fluorescence under the same experimental conditions. In addition, the partition coefficient of the Butein in the PC liposomes wasalso determined by using the fluorescence quenching process. The obtained results can be of biological significance in pharmacology and clinical medicine. © 2015 Elsevier B.V. All rights reserved.