Adsorption mechanism, secondary structure and local distribution of proteins at polyelectrolyte brushes

In many biomedical and biotechnological applications, proteins are immobilized at aqueous-solid interfaces. Generally, an adsorption-induced denaturation of the proteins has to be avoided, because it prevents the use of their biological activity or it might cause adverse effects in living organisms. Furthermore, control over the degree of protein adsorption including protein desorption is extremely useful. Over the recent years, polyelectrolyte brushes have been examined in terms of protein adsorption, and the majority of the studies document their biocompatible properties. Moreover, they show a variable protein affinity responding to the ionic strength of the protein solution. In this short review, selected studies are highlighted that illustrate the most significant properties of polyelectrolyte brushes as adsorbent interfacial structure for proteins.