Design of Bioelectronic Interfaces by Exploiting Hinge-Bending Motions in Proteins
Abstract
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.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Aug 31, 2001
- Source ID
- 10.1126/science.1062461
Entities
People
- David E. Benson
- David W. Conrad
- Homme W. Hellinga
- Lorimier
- Robert M. De
- Scott A Trammell
Organizations
- Duke University Hospital
- United States Naval Research Laboratory