Protein adsorption is a process relevant in many research fields such as biology, medicine and food processing. Its mechanism is influenced by many parameters. Our group has demonstrated that strongly directional interactions induced by ion-bridges connecting individual proteins give rise to a rich phase behaviour including re-entrant condensation and liquid-liquid phase separation (LLPS). Other findings suggest that potential applied to a substrate is able to polarise the adsorbed layer and induce dipole–dipole interactions between the adsorbed and the incoming protein. Building on our recent discovery of ‘re-entrant’ adsorption, we would like to investigate how the surface potential influences the structure (and kinetics) of the adsorption of BSA solutions at high concentrations and in the presence of multivalent ions.