Investigation on 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 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 x 10(-4) cm(2) center dot v(-1) center dot S-1 to-3.046 x 10(-4) center dot cm(2) center dot V-1 center dot s(-1) The binding constant between BSA and liposome was 2. 522 x 10(3) (g/mL) (1) calculated by Scat chard analysis. This method is simple and rapid, and provides a new technology for the investigation on the interactions between protein and liposome.