Human serum albumin in blood detoxification treatment

Abstract

Human serum albumin (HSA) is known to bind a broad spectrum of endogenous and exogenous substances. The ligand-binding property of albumin has been utilized to remove endogenous toxins in extracorporeal blood detoxification methods such as single-pass albumin dialysis (SPAD), fractionated plasma separation and adsorption (FPSA), Prometheus®, and molecular adsorbent recirculating system (MARS). Production of recombinant HSA including individual domains has been successfully attempted by a number of researchers. The albumin domains retain similar structural characteristics of the HSA. The ligand-binding properties of albumin domains are identical to those of HSA but with lower binding affinity and percentage for most of the ligands studied. The albumin domains have an increased elimination profile compared to that of the HSA. Molecular modification of the albumin domains through site-directed mutagenesis for strengthening toxin binding is a feasible approach for improving the efficiency and effectiveness of blood detoxification treatment.