The novel coronavirus disease 2019 (COVID-19) has become a major threat worldwide due to its fast-spreading nature. This disease is caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). The entry of this coronavirus to the host cell is mediated through the transmembrane spike glycoproteins (Hasan et al., 2020). This glycoprotein consists of two subunits and is reported to have a similar affinity to the human angiotensin-converting enzyme 2 (ACE2) as that of the severe acute respiratory syndrome coronavirus (SARS-CoV), which in turn results in efficient spreading of SARS-CoV-2 in humans (Walls et al., 2020). The spike glycol protein binds to its receptor human ACE2 by its receptor-binding domain (RBD) and is activated proteolytically by human protease (Shang et al., 2020). The interaction of the RBD of the spike glycoprotein to ACE2 is carried out by ARG403, TYR453, SER494, TYR495, PHE497, GLN498, THR500, ASN501, TYR505 residues of spike glycoprotein (Lan et al., 2020). The interaction of RBD Spro to ACE2 can be inhibited by the small molecules that interact with the above residues of RBD spike protein (Spro). On the other hand, the SARS-CoV-2 main protease (Mpro), also known as chymotrypsin-like protease, or 3-C-like protease (3CLpro), plays a vital role in processing the polyproteins through the translation of viral RNA. This protease is reported to have a minimum of 11 cleavage sites resulting in viral replication and toxicity (Zhang et al., 2020). The inhibition of these two viral targets can actively block the fusion and replication of SARS-CoV-2.