Design of bioelectronic interfaces by exploiting hinge-bending motions in proteins.

Journal Article (Journal Article)

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.

Full Text

Duke Authors

Cited Authors

  • Benson, DE; Conrad, DW; de Lorimier, RM; Trammell, SA; Hellinga, HW

Published Date

  • August 31, 2001

Published In

Volume / Issue

  • 293 / 5535

Start / End Page

  • 1641 - 1644

PubMed ID

  • 11533486

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1062461


  • eng

Conference Location

  • United States