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General Meathods of Chemical and Electrostatic Control of Protein Binding at Surfaces

Summary: Incorporation of a protein into a novel sensing, electonic, or energy device often requires that the protein be tehtered to an inorganic surface such as an electrode reliably.  There are rigorous requirements for such a system.  1) The surface itself should be clean, well-characterized, and highly reproducible.  2) The protein should be close enough to the surface to engage in electron transfer.  3) The protein should be in a controlled and reproducible orientation, and be physiologically stable over time.  4) Finally, there must be minimal perturbation to protein structure or function.    

There are many creative techniques to bind certain proteins to prepared surfaces, but no completely general strategies that can be used to bind any protein of interest, especially those that have unknown structure or cannot be expressed recombinantly.  The Webb group is developing chemical strategies that attach proteins to surfaces using biological interaction mechanisms.  

Strategy:  The Webb group is developing surface chemical functionalization techniques that use noncovalent binding of proteins through long-range electrostatic forces that mimic biological protein-protein interaction mechanisms.  Using our extensive understanding of the chemical functionalization of ideal surfaces such as silicon and gold, our goal is to prepare surfaces on which small peptide motifs, such as an alpha-helix, beta-sheet, or even random coil, is covalently linked to the surface.  The protein motif carries amino acid side chains that will stabilize protein-protein interactions to present a binding surface to a protein introduced from solution.



By replicating the electrostatic interactions that normally enable large biomolecules to interact and function in a living cell, this strategy will coax proteins to remained folded and fully functional at inorganic substrates, thus integrating the structure and function of that protein with an artificial device.

Stay tuned for more details!




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