Design of Bioelectronic Interfaces by Exploiting Hinge-Bending Motions in Proteins
2001; American Association for the Advancement of Science; Volume: 293; Issue: 5535 Linguagem: Inglês
10.1126/science.1062461
ISSN1095-9203
AutoresDavid E. Benson, David W. Conrad, Robert M. de, Lorimier, Scott A. Trammell, Homme W. Hellinga,
Tópico(s)Neuroscience and Neural Engineering
ResumoWe 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.
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