Physiological interaction of SARS-CoV-2 binding to the ACE-2 receptor

Abstract

For a better knowledge of how viruses enter cells, the associations that are created between the viral glycoproteins and associated human receptors must be studied. The spike glycoprotein (S-glycoprotein) of the new coronavirus SARS-CoV-2 mediates entrance into host cells, and the cellular receptor angiotensin-converting enzyme 2 (ACE-2) has been discovered.The goal of our research was to evaluate the physiological interactions between the SARSCoV-2 and the human cell receptor ACE-2.Modifications were discovered in the S1 monomer of the receptor-binding domain of spikes using an in silico analysis. The observed modifications have a considerable impact on the interlinkage between the SARS-CoV-2 spike and ACE-2.  According to the research outcome, the SARS-Cov-2 spikes proteinhas a strong attraction for the human ACE-2 receptor than the Bat-CoV spikes does. Further, the presence of two loops throughout the SARS-CoV-2 receptor binding domain (RBD) may facilitate binding to the ACE-2 (receptor)throughenhancing the quantity of atoms implicated. The reason SARS-CoV-2 binds to substrates with higher binding energies than SARS-CoV may be due to longer capping loops and changed amino acids.