An impedance sensing platform-combined conducting nanocomposite layer was fabricated to develop an effective and rapid method for detection of coronavirus infection (COVID-19) specific spike receptor binding domain (RBD) protein, a precious antigen marker of COVID-19 disease. Coronavirus infection has spread globally and swiftly with major impacts on health, economy, and quality of life of communities. Fast and reliable detection of COVID-19 is a very significant issue for the effective treatment of this bad illness. For this aim, first, an Epoxy functional group-substituted thiophene monomer was synthesized and electrodeposited on a single-use indium tin oxide (ITO) platform in the presence of acetylene black by employing a cyclic voltammetry technique; thus, a conducting nanocomposite () layer with high conductivity was obtained. This composite was electrodeposited for the first time on the ITO surface to generate a facile and cost-effective impedimetric biosensor. In addition, this composite provided proper attachment points for antibody binding and also supported the biosensor construction. The immuno-specific biointeractions between anti-RBD and RBD proteins hampered the electron transfer between the ITO substrate surface and electrolyte, and this reaction caused variations in impedance signals, and these signals were proportional to the immobilized RBD antigen amounts. The as-prepared immunosensor showed a wide linear dynamic range (0.0012-120 pg/mL), an ultra-low detection limit of 0.58 fg/mL with added superiorities of great selectivity, suitable repeatability, multiple reusability, and excellent reproducibility.
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http://dx.doi.org/10.1021/acsbiomaterials.1c00580 | DOI Listing |
SARS-CoV-2 continues to evolve, with new variants emerging that evade pre-existing immunity and limit the efficacy of existing vaccines. One approach towards developing superior, variant-proof vaccines is to engineer immunogens that preferentially elicit antibodies with broad cross-reactivity against SARS-CoV-2 and its variants by targeting conserved epitopes on spike. The inner and outer faces of the Receptor Binding Domain (RBD) are two such conserved regions targeted by antibodies that recognize diverse human and animal coronaviruses.
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January 2025
Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
A class of tetrahydropyrazino[2,1-a:5,4-a']diisoquinoline derivatives were synthesized under environmentally friendly conditions using water as the solvent. The 3-D structures of some synthesized compounds were determined by X-ray diffraction. Since naturally occurring isoquinoline alkaloids have significant antiviral activities against a wide range of viruses, including coronaviruses, the synthesized compounds were assayed for their inhibitory activities against SARS-CoV-2.
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January 2025
Department of Chemical Sciences, Indian Institute of Science Education and Research Kolkata, Mohanpur, 741246, India.
Developing a broad-spectrum antiviral is imperative in light of the recent emergence of recurring viral infections. The critical role of host-virus attachment and membrane fusion during enveloped virus entry is a suitable target for developing broad-spectrum antivirals. A new class of flavonoid-based fusion inhibitors are designed to alter the membrane's physical properties.
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January 2025
Department of Interface Chemistry and Surface Engineering, Max Planck Institute for Sustainable Materials, 40237, Düsseldorf, Germany.
Biosensors based on DNA aptamer receptors are increasingly used in diagnostic applications. To improve the sensitivity and specificity of aptasensors, parameters affecting the stability and binding efficiency of the receptor layer need to be identified and studied. For example, the blocking step, i.
View Article and Find Full Text PDFAntiviral Res
January 2025
School of Public Health (Shenzhen), Shenzhen Campus of Sun Yat-Sen University, Shenzhen, China; Key Laboratory of Tropical Disease Control (Sun Yat-sen University), Ministry of Education; Shenzhen Key Laboratory of Pathogenic Microbes and Biosafety. Electronic address:
IgA antibodies are critical components of the mucosal immune barrier, providing essential first-line defense against viral infections. In this study, we investigated the impact of antibody class switching on neutralization efficacy by engineering recombinant antibodies of different isotypes (IgA1, IgG1) with identical variable regions from SARS-CoV-2 convalescent patients. A potent, broad-spectrum neutralizing monoclonal antibody CAV-C65 exhibited a ten-fold increase in neutralization potency upon switching from IgG1 to IgA1 monomer.
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