Competitive interfacial adsorption of blood proteins.

The competitive adsorption of blood proteins is of great importance for the treatment of thrombosis using a colloidal drug delivery system. The aim of this study is to investigate competitive adsorption of albumin (BSA) and human immunoglobulin G (HIgG) against fibrinogen (Fb). The competitive adsorption of blood proteins was investigated using interfacial rheology at physiological pH. The influence of bulk concentration, temperature and pH on the interfacial adsorption of protein molecules was determined at the air/aqueous interface. As expected, the results indicated that increase in bulk concentration enhanced the interfacial adsorption. Structure and molecular weight of the protein molecules under investigation had influence on interfacial adsorption leading to a competition at the interface. HIgG is more flexible and surface active molecule than BSA. Thus, HIgG replaced BSA and Fb at the air/aqueous interface. In the presence of Fb, BSA adsorbed rapidly initially and then, was replaced by Fb at the interface. The kinetics of displacement of albumin at the interface was rather slow. In conclusion, the investigation of competitive adsorption of blood proteins may be useful biotechnologically, as it will provide useful information for the production of an antithrombogenic material, which will adsorb albumin rather than Fb.