SARS E blocking peptide

The sudden outbreak due to severe acute respiratory syndrome coronavirus 2 (SARS-Cov-2) is responsible for causing acute. highly dreadful coronavirus disease (COVID-19). The pore-forming proteins in the SARS-CoV-2 en elope protein employ amphipathic alpha-helix for pore formation. The pore openings are essential for the transport of ions. toxins. and viroporin activity. Moreover. there is an insurgence to identify lead compounds to target the novel coronavirus for therapeutic purposes. Therefore in the present study. the SARS-CoV-2 en elope protein sequence was analyzed. constructed the three-dimensional homology model. and screened against the bioactive photochemical Thymoquinone (TO). Molecular docking was performed between the modeled E protein and TO to study protein-ligand interactions using ArgusLab 4.0. The investigation rep Baled that the modeled E protein contains a single alpha-amphipathic helix identified for the first time across the Amino-terminal region of the transmembrane domain may contribute to pore formation of small membrane proteins. Molecular docking results showed the promising inhibitory potential of the ligand TO and the binding free energy of the bound complex as found to be -9.01 kcal/mol. The in silico approach has explicitly demonstrated the significant inhibitory effects of the ligand TO. Therefore it may be used effectively as an antagonist against the SARS- CoV-2 infection owing to its outstanding pharmacological properties.

SARS-CoV-2 has a positive sense RNA genome of 29.9 kb in size, showing high sequence similarity to the BAT-CoV, SARS-CoV, MERS-CoV. SARS-CoV-2 is composed of 14 open reading frames (ORFs), which encodes for a total of 27 proteins divided into structural and non-structural proteins (NSPs). The fundamental structural protein-encoding genes are a spike protein (S) gene, envelope protein (E) gene, a membrane protein (M) gene, and a nucleocapsid protein (N) gene. They make about 33% of the entire genome and are vital for the viral life cycle. Rest 67% is distributed among different NSPs (such as Mpro, helicase, and RNA-dependent RNA polymerase) encoding genes across the ORFs, which are involved in virus-cell receptor interactions during viral entry. Researchers are trying to formulate vaccines, therapeutic antibodies or protein-targeted antiviral drugs to control the spread. This review proceeds stepwise through the COVID-19 outbreak, structural and genomic organization, entry mechanism, pathogenesis, and finally highlighting the essential proteins involved at each step that might be potential targets for drug discovery. Currently, approved treatment modalities consist of only supportive care and oxygen supplementation. This review is established on the current knowledge that has expanded on structural motifs and topology of proteins and their functions. (C) 2020 Published by Elsevier B.V.