Molecular recognition interactions

In fields such as biosensing, analyte binding often relies on very specific molecular recognition interactions that nature has supplied, such as antibody-antigen interactions or strands of complimentary DNA forming double hefices. Unfortunately, because versatile and highly selective receptors for TNT or other explosive molecules are not available, chemists are left to rely on less specific interactions. 

As in all natural and synthetic approaches to molecular recognition, interactions in the surface-confined systems described here are promoted at the ambient/organic interface through both chemical and physical interactions. We have attempted to separate monolayer/molecule interaction phenomena into two distinct problems one chemical and one physical however, it is not possible at present to achieve this degree of segregation. Nevertheless, to the extent that it is possible, we view individual chemical and physical intermolecular interactions as tools that can be used in various combinations to synthesize more complex recognition apparatuses. The size and versatility of our "toolbox" is enhanced if we can quantitatively understand a range of monolayer/molecule interactions. 

The fabrication of nanostructured, multilayer protein films is a prime target for the development of highly efficient sensors or bioreporters, especially where wiring of the biological to a transducer or coupled catalytic sequences are needed [11,22-35]. This has become possible with the advent of layer-by-layer adsorption (LLA) [78,139-146], a procedure based on the deposition of alternate layers of functional macromolecules and proteins, or proteins and proteins, held together by electrostatic, hydrophobic, and/or molecular recognition interactions. 

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