期刊
ACS SENSORS
卷 7, 期 6, 页码 1676-1684出版社
AMER CHEMICAL SOC
DOI: 10.1021/acssensors.2c00317
关键词
electrochemical sensor; nucleocapsid protein; SARS-CoV-2; impedance; label-free detection
资金
- National Research Foundation of Korea (NRF) - Korea government (Ministry of Science and ICT) [NRF-2019R1F1A1062208]
- Ministry of Trade, Industry and Energy [20015793]
- Commercialization Promotion Agency for RD Outcomes [2021-0036]
- Korea Health Industry Development Institute (KHIDI) [HU21C0098]
- Purme Nexon Children Rehabilitation Hospital
This study developed a system for quantifying the nucleocapsid (N) protein in SARS-CoV-2, using an electro-immunosorbent assay and a multichannel impedance analyzer. The system showed highly specific, label-free detection with low cross-reactivity, and allowed for real-time detection of multiple samples.
Diagnosis of coronavirus disease (COVID-19) is important because of the emergence and global spread of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). Real-time polymerase chain reaction (PCR) is widely used to diagnose COVID-19, but it is time-consuming and requires sending samples to test centers. Thus, the need to detect antigens for rapid on-site diagnosis rather than PCR is increasing. We quantified the nucleocapsid (N) protein in SARS-CoV-2 using an electro-immunosorbent assay (El-ISA) and a multichannel impedance analyzer with a 96-interdigitated microelectrode sensor (ToAD). The El-ISA measures impedance signals from residual detection antibodies after sandwich assays and thus offers highly specific, label-free detection of the N protein with low cross-reactivity. The ToAD sensor enables the real-time electrochemical detection of multiple samples in conventional 96-well plates. The limit of detection for the N protein was 0.1 ng/mL with a detection range up to 10 ng/mL. This system did not detect signals for the S protein. While this study focused on detecting the N protein in SARS-CoV-2, our system can also be widely applicable to detecting various biomolecules involved in antigen-antibody interactions.
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