Control of the lateral interactions of immobilized proteins using surface nanoporous-patterning

Protein immobilization on a solid surface is a consequence of complex physical processes at liquid–solid interfaces. Lateral interactions include these physical processes and affect the behavior of proteins at the interfaces. Protein immobilization on planar surfaces frequently produces randomly distributed and irregularly sized protein clusters having large lateral interactions that impair the biochemical functionalities of immobilized proteins. This study discusses control of lateral interactions via nanoporous-patterning of the solid surface. The size of protein clusters and lateral interactions can be controlled via nanoporous-patterning as protein immobilization on a nanoporous surface is confined to the surface that is not occupied by nanopores. Protein clusters on a nanoporous surface are more biochemically functional than clusters on a planar surface.