5 results on '"Ogata, Alana F."'
Search Results
2. Virus Bioresistor (VBR) for Detection of Bladder Cancer Marker DJ‑1 in Urine at 10 pM in One Minute
- Author
-
Bhasin, Apurva, Sanders, Emily C, Ziegler, Joshua M, Briggs, Jeffrey S, Drago, Nicholas P, Attar, Aisha M, Santos, Alicia M, True, Marie Y, Ogata, Alana F, Yoon, Debora V, Majumdar, Sudipta, Wheat, Andrew J, Patterson, Shae V, Weiss, Gregory A, and Penner, Reginald M
- Subjects
Analytical Chemistry ,Chemical Sciences ,Bacteriophage M13 ,Biomarkers ,Tumor ,Biosensing Techniques ,Humans ,Protein Deglycase DJ-1 ,Time Factors ,Urinary Bladder Neoplasms ,Other Chemical Sciences ,Medical biochemistry and metabolomics ,Analytical chemistry ,Chemical engineering - Abstract
DJ-1, a 20.7 kDa protein, is overexpressed in people who have bladder cancer (BC). Its elevated concentration in urine allows it to serve as a marker for BC. However, no biosensor for the detection of DJ-1 has been demonstrated. Here, we describe a virus bioresistor (VBR) capable of detecting DJ-1 in urine at a concentration of 10 pM in 1 min. The VBR consists of a pair of millimeter-scale gold electrodes that measure the electrical impedance of an ultrathin (≈ 150-200 nm), two-layer polymeric channel. The top layer of this channel (90-105 nm in thickness) consists of an electrodeposited virus-PEDOT (PEDOT is poly(3,4-ethylenedioxythiophene)) composite containing embedded M13 virus particles that are engineered to recognize and bind to the target protein of interest, DJ-1. The bottom layer consists of spin-coated PEDOT-PSS (poly(styrenesulfonate)). Together, these two layers constitute a current divider. We demonstrate here that reducing the thickness of the bottom PEDOT-PSS layer increases its resistance and concentrates the resistance drop of the channel in the top virus-PEDOT layer, thereby increasing the sensitivity of the VBR and enabling the detection of DJ-1. Large signal amplitudes coupled with the inherent simplicity of the VBR sensor design result in high signal-to-noise (S/N > 100) and excellent sensor-to-sensor reproducibility characterized by coefficients of variation in the range of 3-7% across the DJ-1 binding curve down to a concentration of 30 pM, near the 10 pM limit of detection (LOD), encompassing four orders of magnitude in concentration.
- Published
- 2020
3. Virus Bioresistor (VBR) for Detection of Bladder Cancer Marker DJ‑1 in Urine at 10 pM in One Minute
- Author
-
Bhasin, Apurva, Sanders, Emily C, Ziegler, Joshua M, Briggs, Jeffrey S, Drago, Nicholas P, Attar, Aisha M, Santos, Alicia M, True, Marie Y, Ogata, Alana F, Yoon, Debora V, Majumdar, Sudipta, Wheat, Andrew J, Patterson, Shae V, Weiss, Gregory A, and Penner, Reginald M
- Subjects
Bacteriophage M13 ,Biomarkers ,Tumor ,Biosensing Techniques ,Humans ,Protein Deglycase DJ-1 ,Time Factors ,Urinary Bladder Neoplasms ,Analytical Chemistry ,Other Chemical Sciences - Abstract
DJ-1, a 20.7 kDa protein, is overexpressed in people who have bladder cancer (BC). Its elevated concentration in urine allows it to serve as a marker for BC. However, no biosensor for the detection of DJ-1 has been demonstrated. Here, we describe a virus bioresistor (VBR) capable of detecting DJ-1 in urine at a concentration of 10 pM in 1 min. The VBR consists of a pair of millimeter-scale gold electrodes that measure the electrical impedance of an ultrathin (≈ 150-200 nm), two-layer polymeric channel. The top layer of this channel (90-105 nm in thickness) consists of an electrodeposited virus-PEDOT (PEDOT is poly(3,4-ethylenedioxythiophene)) composite containing embedded M13 virus particles that are engineered to recognize and bind to the target protein of interest, DJ-1. The bottom layer consists of spin-coated PEDOT-PSS (poly(styrenesulfonate)). Together, these two layers constitute a current divider. We demonstrate here that reducing the thickness of the bottom PEDOT-PSS layer increases its resistance and concentrates the resistance drop of the channel in the top virus-PEDOT layer, thereby increasing the sensitivity of the VBR and enabling the detection of DJ-1. Large signal amplitudes coupled with the inherent simplicity of the VBR sensor design result in high signal-to-noise (S/N > 100) and excellent sensor-to-sensor reproducibility characterized by coefficients of variation in the range of 3-7% across the DJ-1 binding curve down to a concentration of 30 pM, near the 10 pM limit of detection (LOD), encompassing four orders of magnitude in concentration.
- Published
- 2020
4. Virus-Enabled Biosensor for Human Serum Albumin
- Author
-
Ogata, Alana F, Edgar, Joshua M, Majumdar, Sudipta, Briggs, Jeffrey S, Patterson, Shae V, Tan, Ming X, Kudlacek, Stephan T, Schneider, Christine A, Weiss, Gregory A, and Penner, Reginald M
- Subjects
Biotechnology ,Bioengineering ,Bacteriophage M13 ,Biosensing Techniques ,Bridged Bicyclo Compounds ,Heterocyclic ,Electric Conductivity ,Electric Impedance ,Electrodes ,Equipment Design ,Humans ,Limit of Detection ,Polymers ,Reproducibility of Results ,Serum Albumin ,Human ,Virion ,Analytical Chemistry ,Other Chemical Sciences - Abstract
The label-free detection of human serum albumin (HSA) in aqueous buffer is demonstrated using a simple, monolithic, two-electrode electrochemical biosensor. In this device, both millimeter-scale electrodes are coated with a thin layer of a composite containing M13 virus particles and the electronically conductive polymer poly(3,4-ethylenedioxy thiophene) or PEDOT. These virus particles, engineered to selectively bind HSA, serve as receptors in this biosensor. The resistance component of the electrical impedance, Zre, measured between these two electrodes provides electrical transduction of HSA binding to the virus-PEDOT film. The analysis of sample volumes as small as 50 μL is made possible using a microfluidic cell. Upon exposure to HSA, virus-PEDOT films show a prompt increase in Zre within 5 s and a stable Zre signal within 15 min. HSA concentrations in the range from 100 nM to 5 μM are detectable. Sensor-to-sensor reproducibility of the HSA measurement is characterized by a coefficient-of-variance (COV) ranging from 2% to 8% across this entire concentration range. In addition, virus-PEDOT sensors successfully detected HSA in synthetic urine solutions.
- Published
- 2017
5. Virus-Enabled Biosensor for Human Serum Albumin.
- Author
-
Ogata, Alana F, Edgar, Joshua M, Majumdar, Sudipta, Briggs, Jeffrey S, Patterson, Shae V, Tan, Ming X, Kudlacek, Stephan T, Schneider, Christine A, Weiss, Gregory A, and Penner, Reginald M
- Subjects
Humans ,Bacteriophage M13 ,Virion ,Polymers ,Reproducibility of Results ,Equipment Design ,Biosensing Techniques ,Electrodes ,Electric Conductivity ,Electric Impedance ,Limit of Detection ,Bridged Bicyclo Compounds ,Heterocyclic ,Serum Albumin ,Human ,Bridged Bicyclo Compounds ,Heterocyclic ,Serum Albumin ,Human ,Bioengineering ,Biotechnology ,Analytical Chemistry ,Chemical Engineering ,Other Chemical Sciences - Abstract
The label-free detection of human serum albumin (HSA) in aqueous buffer is demonstrated using a simple, monolithic, two-electrode electrochemical biosensor. In this device, both millimeter-scale electrodes are coated with a thin layer of a composite containing M13 virus particles and the electronically conductive polymer poly(3,4-ethylenedioxy thiophene) or PEDOT. These virus particles, engineered to selectively bind HSA, serve as receptors in this biosensor. The resistance component of the electrical impedance, Zre, measured between these two electrodes provides electrical transduction of HSA binding to the virus-PEDOT film. The analysis of sample volumes as small as 50 μL is made possible using a microfluidic cell. Upon exposure to HSA, virus-PEDOT films show a prompt increase in Zre within 5 s and a stable Zre signal within 15 min. HSA concentrations in the range from 100 nM to 5 μM are detectable. Sensor-to-sensor reproducibility of the HSA measurement is characterized by a coefficient-of-variance (COV) ranging from 2% to 8% across this entire concentration range. In addition, virus-PEDOT sensors successfully detected HSA in synthetic urine solutions.
- Published
- 2017
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.