The identification of proteins responsible for cell adhesion, protrusion, and retraction is critical to understanding the process of cell migration. Mass spectrometry is an analytical tool well-suited for detection of proteins and their post-translation modifications. Nevertheless, the majority of mass spectrometry-based methods to study these components rely on solution phase manipulations, even though many of the proteins responsible for mediating cell migration do not function as soluble entities in the cytoplasm. Rather, the inner membrane of a cell provides a unique environment for proteins to assemble into structures called focal adhesion complexes. Cell migration is mediated by the type, number, and contact strength of the adhesions connecting the cell to the surface on which it resides. Therefore, surfaces are a more physiologically relevant medium to study this process. The research proposed here will describe new methods to characterize focal adhesion complexes reconstituted on self-assembled monolayers. These surfaces will be designed to present electroactive moeities that can be used to specifically release the analyte and facilitate detection by mass spectrometry. Finally, hypothesis-driven applications of these methods will be discussed. ? ? ?
