ArticleAngewandte Chemie (Weinheim an der Bergstrasse, Germany)2021
A SARS-CoV-2 Spike Binding DNA Aptamer that Inhibits Pseudovirus Infection by an RBD-Independent Mechanism.
Article in Angewandte Chemie (Weinheim an der Bergstrasse, Germany), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Advances in aptamer technology for target-based drug discovery.Journal of pharmaceutical analysis · 2026Review
- Nucleic acid aptamers in orthopedic diseases: promising therapeutic agents for bone disorders.Bone research · 2025Review
- Non-Covalent Interactions between dUTP C5-Substituents and DNA Polymerase Decrease PCR Efficiency.International journal of molecular sciences · 2023Article
- Mutations of SARS-CoV-2 and their impact on disease diagnosis and severity.Informatics in medicine unlocked · 2023Review
- Functional nucleic acids as modular components against SARS-CoV-2: From diagnosis to therapeutics.Biosensors & bioelectronics · 2022Review
- A Universal DNA Aptamer that Recognizes Spike Proteins of Diverse SARS-CoV-2 Variants of Concern.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Recent advances of functional nucleic acid-based sensors for point-of-care detection of SARS-CoV-2.Mikrochimica acta · 2022Review
- High-Affinity Dimeric Aptamers Enable the Rapid Electrochemical Detection of Wild-Type and B.1.1.7 SARS-CoV-2 in Unprocessed Saliva.Angewandte Chemie (International ed. in English) · 2021Article
- Article
- Discovery and Characterization of Spike N-Terminal Domain-Binding Aptamers for Rapid SARS-CoV-2 Detection.Angewandte Chemie (International ed. in English) · 2021Article
- A SARS-CoV-2 Spike Binding DNA Aptamer that Inhibits Pseudovirus Infection by an RBD-Independent Mechanism.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2021Article
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Authors and funding
7 authors.
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Abstract
The receptor binding domain (RBD) of the spike glycoprotein of the coronavirus SARS-CoV-2 (CoV2-S) binds to the human angiotensin-converting enzyme 2 (ACE2) representing the initial contact point for leveraging the infection cascade. We used an automated selection process and identified an aptamer that specifically interacts with CoV2-S. The aptamer does not bind to the RBD of CoV2-S and does not block the interaction of CoV2-S with ACE2. Nevertheless, infection studies revealed potent and specific inhibition of pseudoviral infection by the aptamer. The present study opens up new vistas in developing SARS-CoV2 infection inhibitors, independent of blocking the ACE2 interaction of the virus, and harnesses aptamers as potential drug candidates and tools to disentangle hitherto inaccessible infection modalities, which is of particular interest in light of the increasing number of escape mutants that are currently being reported.
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