Protein adsorption on colloidal alumina particles functionalized with amino, carboxyl, sulfonate and phosphate groups.

Colloidal oxide particles in biomedical or biotechnological applications immediately become coated with proteins of the biological medium, a process which is strongly influenced by the surface characteristics of the particles. Fundamental correlations between surface characteristics and the, so far mainly uncontrollable, protein adsorption are still not clear. In this study the surface of colloidal alumina particles (d(50)=179 ± 8 nm) was systematically adjusted with NH(2), COOH, SO(3)H and PO(3)H(2) functional groups to investigate the influence on the adsorption of the three model proteins, bovine serum albumin (BSA), lysozyme (LSZ) and trypsin (TRY). The surface functionalization is characterized and discussed in detail with regard to the morphology, isoelectric point, zeta potential, hydrophilic/hydrophobic properties, functional group density and stability. Protein-particle interaction was then assessed by evaluating the amount of protein adsorbed and the zeta potentials of protein-particle conjugates. Protein adsorption was found to be influenced by the type of functional group as well as the expected electrostatic forces under the given experimental conditions. The level of protein adsorption might, hence, be specifically controlled by the type of surface functionalization. Possible adsorption modes of BSA, LSZ and TRY on the particles are suggested by considering the spatial surface potential distribution of the proteins calculated from the protein database file. The particles presented provide an excellent prerequisite for further investigation of fundamental particle-protein interactions and the design of functionally graded materials for biomedical and biotechnological applications, e.g. as drug carriers or for protein purification.