Investigation of the binding affinity of C-terminal domain of SARS coronavirus nucleocapsid protein to nucleotide using AlGaN/GaN high electron mobility transistors

You Ren Hsu; Geng Yen Lee; Jen Inn Chyi; Chung Ke Chang; Chih Cheng Huang; Chen Pin Hsu; Tai Huang Huang; Fan Ren; Yu Lin Wang

doi:10.1109/ICSENS.2012.6411277

Investigation of the binding affinity of C-terminal domain of SARS coronavirus nucleocapsid protein to nucleotide using AlGaN/GaN high electron mobility transistors

You Ren Hsu^*, Geng Yen Lee, Jen Inn Chyi, Chung Ke Chang, Chih Cheng Huang, Chen Pin Hsu, Tai Huang Huang, Fan Ren, Yu Lin Wang

^*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution

2 Citations (Scopus)

Abstract

In this article, we used AlGaN/GaN high electron mobility transistors (HEMTs) to construct the first label-free semiconductor-sensor-based binding assay to our knowledge. Our results suggested that the nucleotide-c terminal domain of SARS coronavirus (SARS-CoV) nucleocapsid protein interaction is a two-step binding event with two dissociation constants (Kd₁ = 0.052 nM, and Kd₂ = 51.24nM) extracted by using the modified two-binding-site Langmuir isotherm equation proposed here. We found that there were at least two protein binding sites on the specific 41-base SARS-CoV double-stranded DNA (dsDNA) genome (29,580-29621) conjugated with a 20-mer poly-dT tail. This result presented a high binding affinity is comparable with the antibody-antigen reaction, and suggested this designed dsDNA could be treated as an aptamer for SARS-CoV N protein capture.

Original language	English
Title of host publication	IEEE SENSORS 2012 - Proceedings
DOIs	https://doi.org/10.1109/ICSENS.2012.6411277
Publication status	Published - 2012
Externally published	Yes
Event	11th IEEE SENSORS 2012 Conference - Taipei, Taiwan Duration: 2012 Oct 28 → 2012 Oct 31

Publication series

Name	Proceedings of IEEE Sensors

Other

Other	11th IEEE SENSORS 2012 Conference
Country/Territory	Taiwan
City	Taipei
Period	2012/10/28 → 2012/10/31

ASJC Scopus subject areas

Electrical and Electronic Engineering

Access to Document

10.1109/ICSENS.2012.6411277

Cite this

Hsu, Y. R., Lee, G. Y., Chyi, J. I., Chang, C. K., Huang, C. C., Hsu, C. P., Huang, T. H., Ren, F., & Wang, Y. L. (2012). Investigation of the binding affinity of C-terminal domain of SARS coronavirus nucleocapsid protein to nucleotide using AlGaN/GaN high electron mobility transistors. In IEEE SENSORS 2012 - Proceedings Article 6411277 (Proceedings of IEEE Sensors). https://doi.org/10.1109/ICSENS.2012.6411277

Investigation of the binding affinity of C-terminal domain of SARS coronavirus nucleocapsid protein to nucleotide using AlGaN/GaN high electron mobility transistors. / Hsu, You Ren; Lee, Geng Yen; Chyi, Jen Inn et al.
IEEE SENSORS 2012 - Proceedings. 2012. 6411277 (Proceedings of IEEE Sensors).

Research output: Chapter in Book/Report/Conference proceeding › Conference contribution

Hsu, YR, Lee, GY, Chyi, JI, Chang, CK, Huang, CC, Hsu, CP, Huang, TH, Ren, F & Wang, YL 2012, Investigation of the binding affinity of C-terminal domain of SARS coronavirus nucleocapsid protein to nucleotide using AlGaN/GaN high electron mobility transistors. in IEEE SENSORS 2012 - Proceedings., 6411277, Proceedings of IEEE Sensors, 11th IEEE SENSORS 2012 Conference, Taipei, Taiwan, 2012/10/28. https://doi.org/10.1109/ICSENS.2012.6411277

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title = "Investigation of the binding affinity of C-terminal domain of SARS coronavirus nucleocapsid protein to nucleotide using AlGaN/GaN high electron mobility transistors",

abstract = "In this article, we used AlGaN/GaN high electron mobility transistors (HEMTs) to construct the first label-free semiconductor-sensor-based binding assay to our knowledge. Our results suggested that the nucleotide-c terminal domain of SARS coronavirus (SARS-CoV) nucleocapsid protein interaction is a two-step binding event with two dissociation constants (Kd1 = 0.052 nM, and Kd2 = 51.24nM) extracted by using the modified two-binding-site Langmuir isotherm equation proposed here. We found that there were at least two protein binding sites on the specific 41-base SARS-CoV double-stranded DNA (dsDNA) genome (29,580-29621) conjugated with a 20-mer poly-dT tail. This result presented a high binding affinity is comparable with the antibody-antigen reaction, and suggested this designed dsDNA could be treated as an aptamer for SARS-CoV N protein capture.",

author = "Hsu, {You Ren} and Lee, {Geng Yen} and Chyi, {Jen Inn} and Chang, {Chung Ke} and Huang, {Chih Cheng} and Hsu, {Chen Pin} and Huang, {Tai Huang} and Fan Ren and Wang, {Yu Lin}",

year = "2012",

doi = "10.1109/ICSENS.2012.6411277",

language = "English",

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AU - Hsu, You Ren

AU - Lee, Geng Yen

AU - Chyi, Jen Inn

AU - Chang, Chung Ke

AU - Huang, Chih Cheng

AU - Hsu, Chen Pin

AU - Huang, Tai Huang

AU - Ren, Fan

AU - Wang, Yu Lin

PY - 2012

Y1 - 2012

N2 - In this article, we used AlGaN/GaN high electron mobility transistors (HEMTs) to construct the first label-free semiconductor-sensor-based binding assay to our knowledge. Our results suggested that the nucleotide-c terminal domain of SARS coronavirus (SARS-CoV) nucleocapsid protein interaction is a two-step binding event with two dissociation constants (Kd1 = 0.052 nM, and Kd2 = 51.24nM) extracted by using the modified two-binding-site Langmuir isotherm equation proposed here. We found that there were at least two protein binding sites on the specific 41-base SARS-CoV double-stranded DNA (dsDNA) genome (29,580-29621) conjugated with a 20-mer poly-dT tail. This result presented a high binding affinity is comparable with the antibody-antigen reaction, and suggested this designed dsDNA could be treated as an aptamer for SARS-CoV N protein capture.

AB - In this article, we used AlGaN/GaN high electron mobility transistors (HEMTs) to construct the first label-free semiconductor-sensor-based binding assay to our knowledge. Our results suggested that the nucleotide-c terminal domain of SARS coronavirus (SARS-CoV) nucleocapsid protein interaction is a two-step binding event with two dissociation constants (Kd1 = 0.052 nM, and Kd2 = 51.24nM) extracted by using the modified two-binding-site Langmuir isotherm equation proposed here. We found that there were at least two protein binding sites on the specific 41-base SARS-CoV double-stranded DNA (dsDNA) genome (29,580-29621) conjugated with a 20-mer poly-dT tail. This result presented a high binding affinity is comparable with the antibody-antigen reaction, and suggested this designed dsDNA could be treated as an aptamer for SARS-CoV N protein capture.

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Investigation of the binding affinity of C-terminal domain of SARS coronavirus nucleocapsid protein to nucleotide using AlGaN/GaN high electron mobility transistors

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