Abstract: A method for the investigation on the interaction between bovine serum albumin (BSA) and liposome using capillary electrophoresis was developed. The oxidation index showed that the liposomes after freeze-drying were more stable. The results obtained from the capillary electrophoretic analysis of liposome showed that liposome had no charge at pH 5.0-8.0. A series of liposome suspension at different concentrations with the internal marker of 0.8% dimethyl sulfoxide (DMSO) were introduced as the electrophoresis buffer at pH 7.0. Along with the liposome concentrations raised from 0 to 2.4 mg/mL, it was found that the effective mobility of BSA changed from -2.232×10-4 cm2·V－1·s－1 to -3.046×10-4 cm2·V－1·s－1. The binding constant between BSA and liposome was 2.522×103(g/mL)-1 calculated by Scatchard analysis. This method is simple and rapid, and provides a new technology for the investigation on the interactions between protein and liposome.

Key words: bovine serum albumin (BSA), liposome , capillary electrophoresis (CE)