Polymer thermodynamics of adsorbed protein layers

Since proteins are polymers, their adsorption at interfaces should share some common features with polymers whose adsorption behavior is being rather well understood using current theoretical approaches. Some theoretical developments are highlighted and recent experimental data obtained mostly with β-casein are compared to them. The general conclusions are that the alternating hydrophilic/hydrophobic block theory gives a general frame for the adsorption of proteins. However, the detailed behavior of proteins at interface seems also influenced by non-covalent, say, electrostatic and hydrogen bonds, whose extent and effects are specified by the local conditions (nature of the fluid phases, temperature, pH, ionic strength, etc.).