Biotin-streptavidin binding interactions of dielectric filled silicon bulk acoustic resonators for smart label-free biochemical sensor applications

Sensor performance of a dielectric filled silicon bulk acoustic resonator type label-free biosensor is verified with biotin-streptavidin binding interactions as a model system. The mass sensor is a micromachined silicon square plate with a dielectric filled capacitive excitation mechanism. The reson...

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Main Authors: Heidari, Amir, Yoon, Yong-Jin, Park, Woo-Tae, Su, Pei-Chen, Miao, Jianmin, Park, Mi Kyoung, Lin, Julius Tsai Ming
Other Authors: School of Mechanical and Aerospace Engineering
Format: Article
Language:English
Published: 2014
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Online Access:https://hdl.handle.net/10356/104974
http://hdl.handle.net/10220/20369
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-1049742023-03-04T17:20:39Z Biotin-streptavidin binding interactions of dielectric filled silicon bulk acoustic resonators for smart label-free biochemical sensor applications Heidari, Amir Yoon, Yong-Jin Park, Woo-Tae Su, Pei-Chen Miao, Jianmin Park, Mi Kyoung Lin, Julius Tsai Ming School of Mechanical and Aerospace Engineering DRNTU::Engineering::Mechanical engineering::Bio-mechatronics Sensor performance of a dielectric filled silicon bulk acoustic resonator type label-free biosensor is verified with biotin-streptavidin binding interactions as a model system. The mass sensor is a micromachined silicon square plate with a dielectric filled capacitive excitation mechanism. The resonance frequency of the biotin modified resonator decreased 315 ppm when exposed to streptavidin solution for 15 min with a concentration of 10−7 M, corresponding to an added mass of 3.43 ng on the resonator surface. An additional control is added by exposing a bovine serum albumin (BSA)-covered device to streptavidin in the absence of the attached biotin. No resonance frequency shift was observed in the control experiment, which confirms the specificity of the detection. The sensor-to-sensor variability is also measured to be 4.3%. Consequently, the developed sensor can be used to observe in biotin-streptavidin interaction without the use of labelling or molecular tags. In addition, biosensor can be used in a variety of different immunoassay tests. Published version 2014-08-21T06:31:55Z 2019-12-06T21:43:52Z 2014-08-21T06:31:55Z 2019-12-06T21:43:52Z 2014 2014 Journal Article Heidari, A., Yoon, Y.-J., Park, W.-T., Su, P.-C., Miao, J., Lin, J. T. M., et al. (2014). Biotin-Streptavidin Binding Interactions of Dielectric Filled Silicon Bulk Acoustic Resonators for Smart Label-Free Biochemical Sensor Applications. Sensors, 14(3), 4585-4598. 1424-8220 https://hdl.handle.net/10356/104974 http://hdl.handle.net/10220/20369 10.3390/s140304585 24608003 en Sensors © 2014 by the authors; licensee MDPI, Basel, Switzerland. This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic DRNTU::Engineering::Mechanical engineering::Bio-mechatronics
spellingShingle DRNTU::Engineering::Mechanical engineering::Bio-mechatronics
Heidari, Amir
Yoon, Yong-Jin
Park, Woo-Tae
Su, Pei-Chen
Miao, Jianmin
Park, Mi Kyoung
Lin, Julius Tsai Ming
Biotin-streptavidin binding interactions of dielectric filled silicon bulk acoustic resonators for smart label-free biochemical sensor applications
description Sensor performance of a dielectric filled silicon bulk acoustic resonator type label-free biosensor is verified with biotin-streptavidin binding interactions as a model system. The mass sensor is a micromachined silicon square plate with a dielectric filled capacitive excitation mechanism. The resonance frequency of the biotin modified resonator decreased 315 ppm when exposed to streptavidin solution for 15 min with a concentration of 10−7 M, corresponding to an added mass of 3.43 ng on the resonator surface. An additional control is added by exposing a bovine serum albumin (BSA)-covered device to streptavidin in the absence of the attached biotin. No resonance frequency shift was observed in the control experiment, which confirms the specificity of the detection. The sensor-to-sensor variability is also measured to be 4.3%. Consequently, the developed sensor can be used to observe in biotin-streptavidin interaction without the use of labelling or molecular tags. In addition, biosensor can be used in a variety of different immunoassay tests.
author2 School of Mechanical and Aerospace Engineering
author_facet School of Mechanical and Aerospace Engineering
Heidari, Amir
Yoon, Yong-Jin
Park, Woo-Tae
Su, Pei-Chen
Miao, Jianmin
Park, Mi Kyoung
Lin, Julius Tsai Ming
format Article
author Heidari, Amir
Yoon, Yong-Jin
Park, Woo-Tae
Su, Pei-Chen
Miao, Jianmin
Park, Mi Kyoung
Lin, Julius Tsai Ming
author_sort Heidari, Amir
title Biotin-streptavidin binding interactions of dielectric filled silicon bulk acoustic resonators for smart label-free biochemical sensor applications
title_short Biotin-streptavidin binding interactions of dielectric filled silicon bulk acoustic resonators for smart label-free biochemical sensor applications
title_full Biotin-streptavidin binding interactions of dielectric filled silicon bulk acoustic resonators for smart label-free biochemical sensor applications
title_fullStr Biotin-streptavidin binding interactions of dielectric filled silicon bulk acoustic resonators for smart label-free biochemical sensor applications
title_full_unstemmed Biotin-streptavidin binding interactions of dielectric filled silicon bulk acoustic resonators for smart label-free biochemical sensor applications
title_sort biotin-streptavidin binding interactions of dielectric filled silicon bulk acoustic resonators for smart label-free biochemical sensor applications
publishDate 2014
url https://hdl.handle.net/10356/104974
http://hdl.handle.net/10220/20369
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