Quantification of Neuropeptide Y with Picomolar Sensitivity Enabled by Guided-Mode Resonance Biosensors

Assessing levels of neuropeptide Y (NPY) in the human body has many medical uses. Accordingly, we report the quantitative detection of NPY biomarkers applying guided-mode resonance (GMR) biosensor methodology. The label-free sensor operates in the near-infrared spectral region exhibiting distinctive...

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Main Authors: Mohammad G. Abdallah, Joseph A. Buchanan-Vega, Kyu J. Lee, Brett R. Wenner, Jeffery W. Allen, Monica S. Allen, Susanne Gimlin, Debra Wawro Weidanz, Robert Magnusson
Format: Article
Language:English
Published: MDPI AG 2019-12-01
Series:Sensors
Subjects:
Online Access:https://www.mdpi.com/1424-8220/20/1/126
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author Mohammad G. Abdallah
Joseph A. Buchanan-Vega
Kyu J. Lee
Brett R. Wenner
Jeffery W. Allen
Monica S. Allen
Susanne Gimlin
Debra Wawro Weidanz
Robert Magnusson
author_facet Mohammad G. Abdallah
Joseph A. Buchanan-Vega
Kyu J. Lee
Brett R. Wenner
Jeffery W. Allen
Monica S. Allen
Susanne Gimlin
Debra Wawro Weidanz
Robert Magnusson
author_sort Mohammad G. Abdallah
collection DOAJ
description Assessing levels of neuropeptide Y (NPY) in the human body has many medical uses. Accordingly, we report the quantitative detection of NPY biomarkers applying guided-mode resonance (GMR) biosensor methodology. The label-free sensor operates in the near-infrared spectral region exhibiting distinctive resonance signatures. The interaction of NPY with bioselective molecules on the sensor surface causes spectral shifts that directly identify the binding event without additional processing. In the experiments described here, NPY antibodies are attached to the sensor surface to impart specificity during operation. For the low concentrations of NPY of interest, we apply a sandwich NPY assay in which the sensor-linked anti-NPY molecule binds with NPY that subsequently binds with anti-NPY to close the sandwich. The sandwich assay achieves a detection limit of ~0.1 pM NPY. The photonic sensor methodology applied here enables expeditious high-throughput data acquisition with high sensitivity and specificity. The entire bioreaction is recorded as a function of time, in contrast to label-based methods with single-point detection. The convenient methodology and results reported are significant, as the NPY detection range of 0.1−10 pM demonstrated is useful in important medical circumstances.
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spelling doaj.art-3c09357e5a4b466b8f9ade01b07150bf2022-12-22T03:18:59ZengMDPI AGSensors1424-82202019-12-0120112610.3390/s20010126s20010126Quantification of Neuropeptide Y with Picomolar Sensitivity Enabled by Guided-Mode Resonance BiosensorsMohammad G. Abdallah0Joseph A. Buchanan-Vega1Kyu J. Lee2Brett R. Wenner3Jeffery W. Allen4Monica S. Allen5Susanne Gimlin6Debra Wawro Weidanz7Robert Magnusson8Department of Electrical Engineering, University of Texas Arlington, Arlington, TX 76019, USADepartment of Electrical Engineering, University of Texas Arlington, Arlington, TX 76019, USADepartment of Electrical Engineering, University of Texas Arlington, Arlington, TX 76019, USAAir Force Research Laboratory, Sensors Directorate, Wright-Patterson AFB, OH 45433, USAAir Force Research Laboratory, Munitions Directorate, Eglin AFB, FL 32542, USAAir Force Research Laboratory, Munitions Directorate, Eglin AFB, FL 32542, USAResonant Sensors Incorporated, Arlington, TX 76010, USAResonant Sensors Incorporated, Arlington, TX 76010, USADepartment of Electrical Engineering, University of Texas Arlington, Arlington, TX 76019, USAAssessing levels of neuropeptide Y (NPY) in the human body has many medical uses. Accordingly, we report the quantitative detection of NPY biomarkers applying guided-mode resonance (GMR) biosensor methodology. The label-free sensor operates in the near-infrared spectral region exhibiting distinctive resonance signatures. The interaction of NPY with bioselective molecules on the sensor surface causes spectral shifts that directly identify the binding event without additional processing. In the experiments described here, NPY antibodies are attached to the sensor surface to impart specificity during operation. For the low concentrations of NPY of interest, we apply a sandwich NPY assay in which the sensor-linked anti-NPY molecule binds with NPY that subsequently binds with anti-NPY to close the sandwich. The sandwich assay achieves a detection limit of ~0.1 pM NPY. The photonic sensor methodology applied here enables expeditious high-throughput data acquisition with high sensitivity and specificity. The entire bioreaction is recorded as a function of time, in contrast to label-based methods with single-point detection. The convenient methodology and results reported are significant, as the NPY detection range of 0.1−10 pM demonstrated is useful in important medical circumstances.https://www.mdpi.com/1424-8220/20/1/126biomarkersguided-mode resonance biosensorneuropeptide yoptical biosensorsandwich assay
spellingShingle Mohammad G. Abdallah
Joseph A. Buchanan-Vega
Kyu J. Lee
Brett R. Wenner
Jeffery W. Allen
Monica S. Allen
Susanne Gimlin
Debra Wawro Weidanz
Robert Magnusson
Quantification of Neuropeptide Y with Picomolar Sensitivity Enabled by Guided-Mode Resonance Biosensors
Sensors
biomarkers
guided-mode resonance biosensor
neuropeptide y
optical biosensor
sandwich assay
title Quantification of Neuropeptide Y with Picomolar Sensitivity Enabled by Guided-Mode Resonance Biosensors
title_full Quantification of Neuropeptide Y with Picomolar Sensitivity Enabled by Guided-Mode Resonance Biosensors
title_fullStr Quantification of Neuropeptide Y with Picomolar Sensitivity Enabled by Guided-Mode Resonance Biosensors
title_full_unstemmed Quantification of Neuropeptide Y with Picomolar Sensitivity Enabled by Guided-Mode Resonance Biosensors
title_short Quantification of Neuropeptide Y with Picomolar Sensitivity Enabled by Guided-Mode Resonance Biosensors
title_sort quantification of neuropeptide y with picomolar sensitivity enabled by guided mode resonance biosensors
topic biomarkers
guided-mode resonance biosensor
neuropeptide y
optical biosensor
sandwich assay
url https://www.mdpi.com/1424-8220/20/1/126
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