Carbon Nanotube Biosensors: Synthesis and Enzymatic Characterization of Protein Modified Nanotubes
1Chemistry Department, University of Massachusetts, Lowell,
Lowell, MA 01854 USA
2Institute of Earth Sciences, Academia Sinica
3Institute of Physics, Academia Sinica
4Department of Physics, PieKing University
This is an abstract
for a presentation given at the
Foresight Conference on Molecular Nanotechnology
Since the report of their discovery in 1991 by Lijima, carbon nanotubes have been extensively studied for their interesting structural, physio-chemical, mechanical, electrical and electromechanical properties. Many potential technological applications have been proposed including, hydrogen storage6, and nanoelectronic devices, field emission display, (FED), field emission microscopy, (FEM)10, and chemical sensors. Since single walled carbon nanotubes may be considered to be molecular wires, their potential use as transducers in sensors is enormous. If combined with the specific recognition properties of immobilized biomolecules these modified carbon nanotubes would provide an ideal platform for miniaturized biosensors. To date, Metallothionein proteins have been trapped inside and placed on the surface of multi-walled nanotubes, Streptavidin was adsorbed on the surface presumably through hydrophobic interactions, and Nucleic Acids have be observed to bind to the surface.
The electronic properties of single-walled carbon nanotubes may be exploited if these molecular wires are modified with molecules that may mediate both molecular recognition and signal tranduction. In constructing a biosensor, the ideal choice for these modifiers would be biomolecules. Potentially enzymes bound to nanotubes represents a selective binding agent that in the presence of a substrate would cause a chemical reaction to act as a signal. To demonstrate the feasibility of such a nanotube-biomolecule construct, we have covalently bound the enzyme alkaline phosphatase with single-walled carbon nanotubes and demonstrated that the enzyme is still active.
Abstract in Microsoft Word® format 20,806 bytes
University of Massachusetts, Lowell
265 Riverside St
Lowell, MA 01854 USA
Phone:  934-3693 Fax:  934-4078