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The molecular structure and cell adhesion properties of the extracellular matrix (ECM) proteins, laminin and fibronectin, were investigated using optical and scanning tunneling microscopy (STM) to assess their potential to construct cellular self-assembly systems useful in molecular device design. Optical micrographs show that both laminin and fibronectin were able to bind cells effectively but only fibronectin was able to effectively interface cells with synthetic microstructures used in the fabrication of a whole cell biosensor. STM was used to gain insight into the molecular structure of these two key ECM proteins as a means to further assess their role in biological cellular assembly. High resolution STM images of these structures were obtained and correlated well with reported molecular structure and dimensions based upon transmission electron microscopy studies. Further, their molecular features were much more evident using STM. Thus, STM can provide the highest resolution yet possible of biological structures in a totally hydrated molecular state. STM offers the potential to study macromolecular self-assembly processes, and possibly their associated universal molecular recognition binding sequences, responsible for cellular self-assembly.

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