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Science 31 August 2001:
Vol. 293. no. 5535, pp. 1641 - 1644
DOI: 10.1126/science.1062461
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Reports

Design of Bioelectronic Interfaces by Exploiting Hinge-Bending Motions in Proteins

David E. Benson,1* David W. Conrad,1 Robert M. de , Lorimier,1 Scott A. Trammell,2 Homme W. Hellinga1dagger

We report a flexible strategy for transducing ligand-binding events into electrochemical responses for a wide variety of proteins. The method exploits ligand-mediated hinge-bending motions, intrinsic to the bacterial periplasmic binding protein superfamily, to establish allosterically controlled interactions between electrode surfaces and redox-active, Ru(II)-labeled proteins. This approach allows the development of protein-based bioelectronic interfaces that respond to a diverse set of analytes. Families of these interfaces can be generated either by exploiting natural binding diversity within the superfamily or by reengineering the specificity of individual proteins. These proteins may have numerous medical, environmental, and defense applications.

1 Department of Biochemistry, Box 3711, Duke University Medical Center, Durham, NC 27710, USA.
2 Center for Biomolecular Science and Engineering, Code 6900, Naval Research Laboratory, Washington, DC 20375, USA.
*   Present address: Wayne State University, Department of Chemistry, Detroit, MI 48202, USA.

dagger    To whom correspondence should be addressed. E-mail: hwh{at}biochem.duke.edu

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