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<p>In this research, structure of SARS-CoV-2 spike glycoprotein S1 and S2 along with TMPRSS2, TMPRSS4, TMPRSS11A, TMPRSS11D and TMPRSS11E serine protease (which activates S1 and S2) are used for docking with repurposed inhibitor drug molecules. We searched for a universally active drug molecule which binds with glycoproteins and serine protease with binding energy above a pre-set threshold value, thus single handedly inhibits the virus glycoprotein interaction with ACE-II receptor on human cell preventing the virus RNA transfer to human cell. Through data analysis performed on binding energies of the selected repurposed inhibitors, we found out five molecules to have high binding energies on both spike glycoproteins and serine protease, while showing less variance in their binding energies. Among these five, Edoxaban is an FDA approved commercially available drug molecule. Hence, high binding molecular inhibitors for spike glycoprotein and serine protease for treatment of SARS-CoV-2 were identified. </p>

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<p>In this research we used the structure of SARS-CoV-2 main protease (Mpro) for docking with Anti-HIV protease inhibitor drug molecules within pH 4-8. By carrying out the variance analysis of binding energies at pH 4-8, it was revealed that the binding energy and mode of interaction of the potential ligands with SARS-CoV-2 Mpro, was dependent on variation of pH. We found out that two of the selected protease inhibitors have differential binding characteristics with changing pH hence their binding energies and mode of interaction depends upon intracellular pH. This differential binding behavior can lead to development of pH selective potent drug molecules for binding with viral protease at lowered intracellular pH of virus infected cell. </p>