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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. Hellinga1
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.
To whom correspondence should be addressed. E-mail:
hwh{at}biochem.duke.edu
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