Investigation on the interaction between bovine serum albumin and liposome using capillary electrophoresis

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 liposomes undergoing 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 increased from 0 to 2.4 mg/mL, it was found that the effective mobility of BSA reduced 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, which was calculated using Scatchard analysis. This method is simple and rapid and provides a new technology for the investigation on the interactions between protein and liposome.