Analytical studies of penicillamine enantiomer surfaces: The molecularly flat surface and the functionality

We fabricated a highly dense protein layer on a self-assembled film of amino acid enantiomers (penicillamine) utilizing a protein-binding interaction to understand the surface structure-induced binding variation. To monitor the self-assembly procedures of the isomers, we modified a previously reported vapor silanization method. The monitoring was conducted by quartz crystal microbalance, surface plasmon resonance and atomic force microscopy techniques. We characterized the assembled surface structure and properties of the isomers using the protein-binding interaction. The results show that a clear difference is existent in the self-assembly procedures and the functionalities of the final films by the molecular chirality. Thus, only one type of the isomers is useful to fabricate a highly dense protein film. In addition, the results show the fabrication of molecularly flat surface relies also on the properties and/or structure of the functional group end of the molecules.