Orientation and Function in Self-Organized Protein Films

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This project, jointly supported by the Division of Chemistry, the Division of Molecular and Cellular Biosciences, and the Division of Biological Instrumentation and Resources, addresses two hypotheses. First, that a highly orientationally ordered, functional protein film can be self-organized by adsorption at a highly ordered liquid/solid interface and that the orientational order of this film can be controlled by changing the nature of this interface, and second, that biochemical function in a protein film is dependent on macroscopic orientational order. The objective of this study is to provide a more detailed understanding of protein films for applications in biosensing and bioseparations devices. During the tenure of this thirty-four month continuing grant, Professor Saavedra, a chemist, and Dr. Li, an optical scientist, will cooperatively apply polarized reflection spectroscopies, namely planar integrated optical waveguide-attenuated total reflection (IOW-ATR) and total internal reflection fluorescence (TIRF), to the in situ characterization of the structure and function of cytochrome c and myoglobin films at the solid-liquid interface. This research addresses both the preparation of ordered, functional protein films and the development of analytical techniques appropriate to characterize these films. The successful development of a general methodology to self-organize proteins into oriented two-dimensional arrays would be highly useful for biotechnological applications. Also, this research should give rise to a clearer understanding of relationships between the structure of hydrated protein films and their macroscopic properties which should aid in protein film design and applications.