Molecular recognition on the supported and on the air/water interface-spread protein monolayers

Targeting of proteins at interfaces via affinity ligands or specific antibodies is important for the understanding of protein functioning in biological membranes. This review brings together a great number of research works accomplished in this field in the past decade by a variety of analytical methods. It highlights two simple in situ techniques of monitoring molecular recognition processes at interfaces recently developed in the author's laboratory. The first of these techniques is based on the measurements of surface pressure increments of a protein monolayer spread at the air/water interface at a constant area resulting from the interaction with its specific ligands injected into the aqueous subphase beneath the preformed protein monolayer. The second technique takes advantage of the feature of [14C]-labeled proteins that enable in situ measurements of surface density changes of adsorbed protein molecules on a solid support resulting from the interaction with its specific antibody.