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Electrochemical biosensor for the evaluation of monoclonal antibodies targeting the N protein of SARS-CoV-2 virus.
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- Author(s): Liustrovaite V;Liustrovaite V;Liustrovaite V; Drobysh M; Drobysh M; Drobysh M; Ratautaite V; Ratautaite V; Ramanaviciene A; Ramanaviciene A; Rimkute A; Rimkute A; Simanavicius M; Simanavicius M; Dalgediene I; Dalgediene I; Kucinskaite-Kodze I; Kucinskaite-Kodze I; Plikusiene I; Plikusiene I; Chen CF; Chen CF; Viter R; Viter R; Viter R; Ramanavicius A; Ramanavicius A; Ramanavicius A
- Source:
The Science of the total environment [Sci Total Environ] 2024 May 10; Vol. 924, pp. 171042. Date of Electronic Publication: 2024 Feb 16.- Publication Type:
Journal Article- Language:
English - Source:
- Additional Information
- Source: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 0330500 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1879-1026 (Electronic) Linking ISSN: 00489697 NLM ISO Abbreviation: Sci Total Environ Subsets: MEDLINE
- Publication Information: Original Publication: Amsterdam, Elsevier.
- Subject Terms:
- Abstract: The emergence of COVID-19 caused by the coronavirus SARS-CoV-2 has prompted a global pandemic that requires continuous research and monitoring. This study presents a design of an electrochemical biosensing platform suitable for the evaluation of monoclonal antibodies targeting the SARS-CoV-2 nucleocapsid (N) protein. Screen-printed carbon electrodes (SPCE) modified with gold nanostructures (AuNS) were applied to design a versatile and sensitive sensing platform. Electrochemical techniques, including electrochemical impedance spectroscopy (EIS) and square wave voltammetry (SWV), were used to investigate the interactions between immobilised recombinant N (rN) protein and several monoclonal antibodies (mAbs). The electrochemical characterisation of SPCE/AuNS/rN demonstrated a successful immobilisation of rN, enhancing the electron transfer kinetics. Affinity interactions between immobilised rN and four mAbs (mAb-4B3, mAb-4G6, mAb-12B2, and mAb-1G5) were explored. Although mAb-4B3 showed some non-linearity, the other monoclonal antibodies exhibited specific and well-defined interactions followed by the formation of an immune complex. The biosensing platform demonstrated high sensitivity in the linear range (LR) from 0.2 nM to 1 nM with limits of detection (LOD) ranging from 0.012 nM to 0.016 nM for mAb-4G6, mAb-12B2, and mAb-1G5 and limits of quantification (LOQ) values ranging from 0.035 nM to 0.139 nM, as determined by both EIS and SWV methods. These results highlight the system's potential for precise and selective detection of monoclonal antibodies specific to the rN. This electrochemical biosensing platform provides a promising route for the sensitive and accurate detection of monoclonal antibodies specific to the rN protein.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 Elsevier B.V. All rights reserved.) - Contributed Indexing: Keywords: Bioelectrochemistry; Immunoanalysis; Immunosensor; Interaction kinetics; N protein; SARS-CoV-2 virus; Specific antibodies
- Accession Number: 0 (Antibodies, Monoclonal)
7440-44-0 (Carbon) - Publication Date: Date Created: 20240218 Date Completed: 20240403 Latest Revision: 20240403
- Publication Date: 20240403
- Accession Number: 10.1016/j.scitotenv.2024.171042
- Accession Number: 38369150
- Source:
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