Structural Insight into the Binding of Cyanovirin-N with the Spike Glycoprotein, Mpro and PLpro of SARS-CoV-2: Protein–Protein Interactions, Dynamics Simulations and Free Energy Calculations
The emergence of COVID-19 continues to pose severe threats to global public health. The pandemic has infected over 171 million people and claimed more than 3.5 million lives to date. We investigated the binding potential of antiviral cyanobacterial proteins including cyanovirin-N, scytovirin and...
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| Format: | Article |
| Idioma: | anglès |
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MPDI
2025
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| Accés en línia: | https://repository.auw.edu.bd/handle/123456789/782 |
| _version_ | 1857449040257482752 |
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| author | Roy, Ayan |
| author_facet | Roy, Ayan |
| author_sort | Roy, Ayan |
| collection | institutional Repository |
| description | The emergence of COVID-19 continues to pose severe threats to global public health. The
pandemic has infected over 171 million people and claimed more than 3.5 million lives to date.
We investigated the binding potential of antiviral cyanobacterial proteins including cyanovirin-N,
scytovirin and phycocyanin with fundamental proteins involved in attachment and replication of
SARS-CoV-2. Cyanovirin-N displayed the highest binding energy scores (−16.8 ± 0.02 kcal/mol,
−12.3 ± 0.03 kcal/mol and −13.4 ± 0.02 kcal/mol, respectively) with the spike protein, the main
protease (Mpro) and the papainlike protease (PLpro) of SARS-CoV-2. Cyanovirin-N was observed to
interact with the crucial residues involved in the attachment of the human ACE2 receptor. Analysis of
the binding affinities calculated employing the molecular mechanics-Poisson–Boltzmann surface area
(MM-PBSA) approach revealed that all forms of energy, except the polar solvation energy, favourably
contributed to the interactions of cyanovirin-N with the viral proteins. With particular emphasis
on cyanovirin-N, the current work presents evidence for the potential inhibition of SARS-CoV-2 by
cyanobacterial proteins, and offers the opportunity for in vitro and in vivo experiments to deploy
the cyanobacterial proteins as valuable therapeutics against COVID-19. |
| format | Article |
| id | 123456789-782 |
| institution | Asian University for Women |
| language | English |
| publishDate | 2025 |
| publisher | MPDI |
| record_format | dspace |
| spelling | 123456789-7822026-02-18T06:15:08Z Structural Insight into the Binding of Cyanovirin-N with the Spike Glycoprotein, Mpro and PLpro of SARS-CoV-2: Protein–Protein Interactions, Dynamics Simulations and Free Energy Calculations Roy, Ayan SARS-CoV-2; spike protein; Mpro; PLpro; cyanobacteria; cyanovirin-N; scytovirin; phyco- cyanin; molecular docking; molecular dynamics simulations The emergence of COVID-19 continues to pose severe threats to global public health. The pandemic has infected over 171 million people and claimed more than 3.5 million lives to date. We investigated the binding potential of antiviral cyanobacterial proteins including cyanovirin-N, scytovirin and phycocyanin with fundamental proteins involved in attachment and replication of SARS-CoV-2. Cyanovirin-N displayed the highest binding energy scores (−16.8 ± 0.02 kcal/mol, −12.3 ± 0.03 kcal/mol and −13.4 ± 0.02 kcal/mol, respectively) with the spike protein, the main protease (Mpro) and the papainlike protease (PLpro) of SARS-CoV-2. Cyanovirin-N was observed to interact with the crucial residues involved in the attachment of the human ACE2 receptor. Analysis of the binding affinities calculated employing the molecular mechanics-Poisson–Boltzmann surface area (MM-PBSA) approach revealed that all forms of energy, except the polar solvation energy, favourably contributed to the interactions of cyanovirin-N with the viral proteins. With particular emphasis on cyanovirin-N, the current work presents evidence for the potential inhibition of SARS-CoV-2 by cyanobacterial proteins, and offers the opportunity for in vitro and in vivo experiments to deploy the cyanobacterial proteins as valuable therapeutics against COVID-19. 2025-07-24T07:51:56Z 2025-07-24T07:51:56Z 2021 Article https://repository.auw.edu.bd/handle/123456789/782 en application/pdf MPDI |
| spellingShingle | SARS-CoV-2; spike protein; Mpro; PLpro; cyanobacteria; cyanovirin-N; scytovirin; phyco- cyanin; molecular docking; molecular dynamics simulations Roy, Ayan Structural Insight into the Binding of Cyanovirin-N with the Spike Glycoprotein, Mpro and PLpro of SARS-CoV-2: Protein–Protein Interactions, Dynamics Simulations and Free Energy Calculations |
| title | Structural Insight into the Binding of Cyanovirin-N with the Spike Glycoprotein, Mpro and PLpro of SARS-CoV-2: Protein–Protein Interactions, Dynamics Simulations and Free Energy Calculations |
| title_full | Structural Insight into the Binding of Cyanovirin-N with the Spike Glycoprotein, Mpro and PLpro of SARS-CoV-2: Protein–Protein Interactions, Dynamics Simulations and Free Energy Calculations |
| title_fullStr | Structural Insight into the Binding of Cyanovirin-N with the Spike Glycoprotein, Mpro and PLpro of SARS-CoV-2: Protein–Protein Interactions, Dynamics Simulations and Free Energy Calculations |
| title_full_unstemmed | Structural Insight into the Binding of Cyanovirin-N with the Spike Glycoprotein, Mpro and PLpro of SARS-CoV-2: Protein–Protein Interactions, Dynamics Simulations and Free Energy Calculations |
| title_short | Structural Insight into the Binding of Cyanovirin-N with the Spike Glycoprotein, Mpro and PLpro of SARS-CoV-2: Protein–Protein Interactions, Dynamics Simulations and Free Energy Calculations |
| title_sort | structural insight into the binding of cyanovirin n with the spike glycoprotein mpro and plpro of sars cov 2 protein protein interactions dynamics simulations and free energy calculations |
| topic | SARS-CoV-2; spike protein; Mpro; PLpro; cyanobacteria; cyanovirin-N; scytovirin; phyco- cyanin; molecular docking; molecular dynamics simulations |
| url | https://repository.auw.edu.bd/handle/123456789/782 |
| work_keys_str_mv | AT royayan structuralinsightintothebindingofcyanovirinnwiththespikeglycoproteinmproandplproofsarscov2proteinproteininteractionsdynamicssimulationsandfreeenergycalculations |