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Liposomes have hydrophilic and hydrophobic properties with a two-layer membrane structure.In vivo environments,proteins are mostlyenclosed in membranes.Adding liposomes in the buffers of capillary electrophoresis(CE) as pseudo-stationary phase could establish a biological circumstance to study the interaction of liposomes with proteins[1].α-glucosidase is an effective target enzyme for diabetes.The inhibitors of α-glucosidase could weaken the violent hydrolysis reaction of carbohydrates into glucoses,which eventually caused drop of the postprandial glucose level in blood.Human Serum Albumin (HSA) is the most abundant and important carrier protein in blood plasma.When medicines enter into the blood plasma,it will bind with HSA,which can bring it to different parts in human body to alleviate or cure diseases and injuries[2].Liposomes were prepared by rotary evaporation,sonication and breaking.The average size was 84.71 nm and the Zeta potential of liposome was -50.9mV,which showed that liposome suspensions were a relatively stable system.We used CE to determine the binding constant between liposome and α-glucosidase or HSA.CE was performed using gradients concentrations of liposomes as running buffer (pH=7.4).4-Methyl-2-pentanone (MO) was added into the sample so as to get the effect of electroosmotic flow of CE.The constant was calculated by mobility shift method.The binding constants of α-glucosidase and HSA with liposomes were determined to be 1.99×104(g/ml)-1(Fig.1) and 5.10×103(g/ml)-1(Fig.2).The study is necessary as the research on interactions between proteins and liposomes provides the foundation for interaction between medicine and Liposome-protein compounds.The state of protein compounds is similar to the real vivo environment than pure proteins without membranes.