ArticleFrontiers in molecular biosciences2021
DNA Aptamers Block the Receptor Binding Domain at the Spike Protein of SARS-CoV-2.
Article in Frontiers in molecular biosciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- Designing the Future of Biosensing: Advances in Aptamer Discovery, Computational Modeling, and Diagnostic Applications.Biosensors · 2025Review
- Molecular dynamics simulations reveal mechanistic insights into aptamer-induced structural rearrangements in viral capsid proteins.Journal of computer-aided molecular design · 2025Article
- Comparative Analysis of Aptamer-Conjugated Chemical and Green Synthesized Gold Nanoparticles for Targeted Therapy in MCF-7 Cancer Cells.Applied biochemistry and biotechnology · 2025Article
- Enhancing Target Detection: A Fluorescence-Based Streptavidin-Bead Displacement Assay.Biosensors · 2024Article
- Cooperative dynamics of PARP-1 zinc-finger domains in the detection of DNA single-strand breaks.Scientific reports · 2024Article
- Characterizing Aptamer Interaction with the Oncolytic Virus VV-GMCSF-Lact.Molecules (Basel, Switzerland) · 2024Article
- Article
- Aptamer-based Emerging Tools for Viral Biomarker Detection: A Focus on SARS-CoV-2.Current medicinal chemistry · 2023Review
- In-Silico Selection of Aptamer Targeting SARS-CoV-2 Spike Protein.International journal of molecular sciences · 2022Article
- Aptamers as promising nanotheranostic tools in the COVID-19 pandemic era.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2022Review
- Glycosylation of Receptor Binding Domain of SARS-CoV-2 S-Protein Influences on Binding to Immobilized DNA Aptamers.International journal of molecular sciences · 2022Article
- Advances to tackle backbone flexibility in protein docking.Current opinion in structural biology · 2021Review
- Review
- DNA Aptamers Block the Receptor Binding Domain at the Spike Protein of SARS-CoV-2.Frontiers in molecular biosciences · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA aptamers are versatile molecular species obtained by the folding of short single-stranded nucleotide sequences, with highly specific recognition capabilities against proteins. Here we test the ability of DNA aptamers to interact with the spike (S-)protein of the SARS-CoV-2 viral capsid. The S-protein, a trimer made up of several subdomains, develops the crucial function of recognizing the ACE2 receptors on the surface of human cells, and subsequent fusioning of the virus membrane with the host cell membrane. In order to achieve this, the S1 domain of one protomer switches between a closed conformation, in which the binding site is inaccessible to the cell receptors, and an open conformation, in which ACE2 can bind, thereby initiating the entry process of the viral genetic material in the host cell. Here we show, by means of state-of-the-art molecular simulations, that small DNA aptamers experimentally identified can recognize the S-protein of SARS-CoV-2, and characterize the details of the binding process. We find that their interaction with different subdomains of the S-protein can effectively block, or at least considerably slow down the opening process of the S1 domain, thereby significantly reducing the probability of virus-cell binding. We provide evidence that, as a consequence, binding of the human ACE2 receptor may be crucially affected under such conditions. Given the facility and low cost of fabrication of specific aptamers, the present findings could open the way to both an innovative viral screening technique with sub-nanomolar sensitivity, and to an effective and low impact curative strategy.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.