Fluorescence correlation spectroscopy and solid supported biomimetic sensing platforms are a suitable method for studying the underlying chemical physics of receptor-ligand binding interactions. These strategies are used in conjunction with naturally occurring transmembrane proteins incorporated into phospholipid bilayers on the surface of porous silica beads. Incorporating the receptor proteins into this type of solid support allows for the native multivalent analyte recognition capability of the protein while simplifying the direct spectroscopic observation of binding events. The protein analyte interaction for the systems of interest result in a change in protein quaternary structure which results in extremely high binding affinities and enhanced selectivity. The microenvironment of these proteins and the thermodynamic properties of the bilayer will determine the overall utility of this system. Strategies for determining these parameters for a novel biosensing platform will be presented.

The detection strategies for the determination of analyte presence are based upon well understood chemical physical parameters that utilize the change in protein structure upon binding to bring about a gross change in observables. Examples of these physical parameters are the distance between protein subunits or a change in diffusion coefficient within the bilayer for the subunits upon analyte binding. This allows for the direct determination of binding events rather than relying upon downstream events as a sensing approach. Additionally, due to the inherently selective nature of multivalent analyte recognition, pretreatment steps required in many sensing strategies can be neglected. This provides for a sensing methodology that is sensitive while being inherently simple.