SENSOR SURFACE INTERACTIONS IN THE STUDY OF MACROMOLECULAR ASSEMBLIES

Macromolecular assemblies, like viruses, are often built by multiple copies of a few components. These may have similar or diverse functions. The multivalency of the assembly allows ligand recognition with high avidity. Nevertheless, affinity is linked to the monovalent ligand interaction, related to the nature of the interactive surface. Such interactions can be followed in real time by the aid of surface plasmon resonance. Thus a sensor surface may be prepared with either the assembly or the ligand immobilized at the sensor and their interaction studied. Kinetic and thermodynamic properties of ligand binding to the macro-molecular assembly can be determined. Variations in the structure of the assembly, like those occurring during virus infection may also be revealed by this technique.