
Ebola virus infections cause hemorrhagic fever that often results in very high fatality rates. In addition to exploring vaccines, development of drugs is also essential for treating the disease and preventing the spread of the infection. The Ebola virus matrix protein VP40 exists in various conformational and oligomeric forms and is a potential pharmacological target for disrupting the virus life-cycle. Here we explored graphene-VP40 interactions using molecular dynamics simulations and graphene pelleting assays. We found that graphene sheets associate strongly with VP40 at various interfaces. We also found that the graphene is able to disrupt the C-terminal domain (CTD-CTD) interface of VP40 hexamers. This VP40 hexamer-hexamer interface is crucial in forming the Ebola viral matrix and disruption of this interface may provide a method to use graphene or similar nanoparticle based solutions as a disinfectant that can significantly reduce the spread of the disease and prevent an Ebola epidemic.
Binding Sites, graphene-VP40, Protein Conformation, Viral Core Proteins, interactions, Molecular Dynamics Simulation, Viral Matrix Proteins, Ebola virus, Nucleoproteins, Graphite, Protein Multimerization, Protein Binding
Binding Sites, graphene-VP40, Protein Conformation, Viral Core Proteins, interactions, Molecular Dynamics Simulation, Viral Matrix Proteins, Ebola virus, Nucleoproteins, Graphite, Protein Multimerization, Protein Binding
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