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The Virus Bioresistor: Wiring Virus Particles for the Direct, Label-Free Detection of Target Proteins.
- Source :
-
Nano Letters . 6/13/2018, Vol. 18 Issue 6, p3623-3629. 7p. - Publication Year :
- 2018
-
Abstract
- The virus bioresistor (VBR) is a chemiresistor that directly transfers information from virus particles to an electrical circuit. Specifically, the VBR enables the label-free detection of a target protein that is recognized and bound by filamentous M13 virus particles, each with dimensions of 6 nm (w) × 1 μm (l), entrained in an ultrathin (~250 nm) composite virus-polymer resistor. Signal produced by the specific binding of virus to target molecules is monitored using the electrical impedance of the VBR: The VBR presents a complex impedance that is modeled by an equivalent circuit containing just three circuit elements: a solution resistance (Rsoln), a channel resistance (RVBR), and an interfacial capacitance (CVBR). The value of RVBR, measured across 5 orders of magnitude in frequency, is increased by the specific recognition and binding of a target protein to the virus particles in the resistor, producing a signal ΔRVBR. The VBR concept is demonstrated using a model system in which human serum albumin (HSA, 66 kDa) is detected in a phosphate buffer solution. The VBR cleanly discriminates between a change in the electrical resistance of the buffer, measured by Rsoln, and selective binding of HSA to virus particles, measured by RVBR. The ΔRVBR induced by HSA binding is as high as 200 Ω, contributing to low sensor-to-sensor coefficients-of-variation (<15%) across the entire calibration curve for HSA from 7.5 nM to 900 nM. The response time for the VBR is 3-30 s. [ABSTRACT FROM AUTHOR]
- Subjects :
- *ELECTRIC circuits
*PROTEINS
*ELECTRIC capacity
*PARTICLES
*SERUM albumin
Subjects
Details
- Language :
- English
- ISSN :
- 15306984
- Volume :
- 18
- Issue :
- 6
- Database :
- Academic Search Index
- Journal :
- Nano Letters
- Publication Type :
- Academic Journal
- Accession number :
- 130252354
- Full Text :
- https://doi.org/10.1021/acs.nanolett.8b00723