ArticleJournal of molecular liquids2022
A molecular dynamic study on the ability of phosphorene for designing new sensor for SARS-CoV-2 detection.
Article in Journal of molecular liquids, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 20 citations in OpenAlex.
- Multi-scale computational insights into West Nile virus E-protein adsorption on graphene and phosphorene nanomaterials.Nanoscale advances · 2026Article
- Gold Nanoparticle-Based Systems for Targeting the Ara h2 Allergen: A Molecular Modeling Approach.Computational and structural biotechnology journal · 2026Article
- 3D-QSAR and Molecular Dynamics Study of Isoxazole Derivatives to Identify the Structural Requirements for Farnesoid X Receptor (FXR) Agonists.Molecules (Basel, Switzerland) · 2024Article
- Identification of microbes using single-layer graphene-based nano biosensors.Journal of molecular modeling · 2023Article
- Theoretical Evaluation of Potential Cytotoxicity of Graphene Quantum Dot to Adsorbed DNA.Materials (Basel, Switzerland) · 2022Article
- Methodology-Centered Review of Molecular Modeling, Simulation, and Prediction of SARS-CoV-2.Chemical reviews · 2022Review
- A molecular dynamic study on the ability of phosphorene for designing new sensor for SARS-CoV-2 detection.Journal of molecular liquids · 2022Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Due to the dramatic increase in the number of patients with severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), designing new selective and sensitive sensors for the detection of this virus is of importance. In this research, by employing full atomistic molecular dynamics (MD) simulations, the interactions of the receptor-binding domain (RBD) of the SARS-CoV-2 with phosphorene and graphene nanosheets were analyzed to investigate their sensing ability against this protein. Based on the obtained results, the RBD interactions with the surface of graphene and phosphorene nanosheets do not have important effects on the folding properties of the RBD but this protein has unique dynamical behavior against each nanostructure. In the presence of graphene and phosphorene, the RBD has lower stability because due to the strong interactions between RBD and these nanostructures. This protein spreads on the surface and has lower structural compaction, but in comparison with graphene, RBD shows greater stability on the surface of the phosphorene nanosheet. Moreover, RBD forms a more stable complex with phosphorene nanosheet in comparison with graphene due to greater electrostatic and van der Waals interactions. The calculated Gibbs binding energy for the RBD complexation process with phosphorene and graphene are -200.37 and -83.65 kcal mol
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