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
| Autor: | Akash Anandraj, Taurai Mutanda, Arnab Sen, Ayan Roy, Joseph K. Bwapwa, Devashan Naidoo, Pallab Kar |
|---|---|
| Rok vydání: | 2022 |
| Předmět: |
medicine.medical_treatment
Binding energy Pharmaceutical Science Organic chemistry Coronavirus Papain-Like Proteases Plasma protein binding spike protein cyanobacteria PLpro Analytical Chemistry chemistry.chemical_compound QD241-441 X-Ray Diffraction Drug Discovery Protein Interaction Mapping Coronavirus 3C Proteases Scytovirin chemistry.chemical_classification scytovirin biology Chemistry phycocyanin Molecular Docking Simulation Cyanovirin-N Coronavirus Protease Inhibitors Biochemistry Chemistry (miscellaneous) Spike Glycoprotein Coronavirus Molecular Medicine Mpro Protein Binding Biotechnology Molecular Dynamics Simulation Antiviral Agents Article Protein–protein interaction Bacterial Proteins medicine Humans Physical and Theoretical Chemistry cyanovirin-N Protease SARS-CoV-2 COVID-19 molecular docking molecular dynamics simulations In vitro COVID-19 Drug Treatment biology.protein Glycoprotein |
| Zdroj: | Molecules Volume 26 Issue 17 Molecules, Vol 26, Iss 5114, p 5114 (2021) |
| DOI: | 10.48741/mut.18758942 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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