Capillary electrophoresis as a useful analytical tool for the characterization of hollow-fiber membrane-supported hydrogels for the design of a bioartificial extra-corporeal liver

VIZIOLI NM

Santiago de Chile, Chile

Simposio; 13th Symposium on Biomedical, Biopharmaceutical and Industrial Applications of Capillary Electrophoresis and Microchip Technology; 2007

For the treatment of human patients with terminal hepatic diseases, such as acute liver or metabolic liver diseases, the therapy of choice is whole-organ transplantation. In addition, there are short-term therapies either to recover the essential functions of the liver in fault, or to maintain the patient during the critical period of the disease until the transplant can be carried out. In order to implement a practical clinical solution many  research groups have attempted to develop different extra-corporeal bioartificial liver (BAL) system. Typically, a BAL system is a bioreactor where hepatic cells perform the hepatic functions by processing the blood or plasma of patients with liver failure. The hepatic cells are separated from the surrounding media by porous polymeric membranes which control the exchange of substances by mass transfer processes such as convection, diffusion and osmosis. The present study focuses on the design of  radiation-induced in situ synthesis of hydrogels confined to the macroporous structure of hollow-fiber membranes. Different chemical composition hydrogels were synthesized and characterized by their mass transport properties. In this context, capillary electrophoresis offered once again its recognized advantages of high resolution, rapid analysis and small sample consumption. Albumin and immunoglobulin concentrations were determined at different times in a receiving reservoir by capillary electrophoresis. Acrylamide-based hydrogels showed a differential behavior in the permeabilities of proteins with different molecular weight, allowing higher permeabilities  to low molecular weight proteins as albumin and restriction enhanced barrier to immunoglobulin G, responsible of triggering the humoral immunity response.