In this in vitro study, carbonic anhydrase-liposome complex was prepared to simulate the in vivo interactions between drug molecules and carbonic anhydrase. The complex was prepared by ultrasonic cell disruption, mixing and extrusion. Zeta potential and the size of carbonic anhydrase-liposome complex were -45.06 mV and 99.43 nm, respectively, indicating this complex is stable and suitable to apply for capillary electrophoresis. The complex was further added in running buffers as pseudo stationary phase in capillary electrophoresis, and 4-carboxybenzenesulfonamide (containing 2.2×10^-3 mol/L 4-methyl-2-pentanone as EOF marker) was added as a sample to establish the model of the interaction between the drug and carbonic anhydrase-liposome complex using Scatchard method. The binding constant in this model was 1.172×10⁴mL·g^-1. Among the 12 drugs studied using this method, caffeic acid, L-ascorbic acid, 2,4-dichloro-5-sulfamoylbenzoic acid, and 4-chloro-3-sulfamoyl benzoic acid had strong interactions with carbonic anhydrase-liposome complex, having higher binding constants than that of 4-carboxybenzenesulfonamide. Ferulic acid, aristolochic acid, gallic acid, protocatechuic acid, and nicotinic acid had weak interactions with carbonic anhydrase-liposome complex, having lower binding constants than that of 4-carboxybenzenesulfonamide. This method can be used to check interactions between carbonic anhydrase or other targets and drug molecules rapidly and effectively, reducing the development cycle of drugs.

liposome  /  carbonic anhydrase  /  capillary electrophoresis