Abstract
The ability of coronaviruses to infect humans is invariably associated with their binding strengths to human receptor proteins. Both SARS-CoV-2, initially named 2019-nCoV, and SARS-CoV were reported to utilize angiotensin-converting enzyme 2 (ACE2) as an entry receptor in human cells. To better understand the interplay between SARS-CoV-2 and ACE2, we performed computational alanine scanning mutagenesis on the “hotspot” residues at protein-protein interfaces using relative free energy calculations. Our data suggest that the mutations in SARS-CoV-2 lead to a greater binding affinity relative to SARS-CoV. In addition, our free energy calculations provide insight into the infectious ability of viruses on a physical basis and also provide useful information for the design of antiviral drugs.
【초록키워드】 viruses, SARS-CoV-2, ACE2, coronavirus, Mutation, SARS-CoV, Human, antiviral drugs, 2019-nCoV, virus, angiotensin-converting enzyme 2, binding affinity, Free energy calculation, free energy, Free energy calculations, information, binding, Angiotensin-converting enzyme, Mutagenesis, angiotensin, lead, residue, human cells, Alanine, entry receptor, nCoV, receptor proteins, infect, physical, protein-protein interface, protein-protein interfaces, greater, performed, reported, addition, 【제목키워드】 SARS-CoV-2, prediction, energy, relative, calculation, Effect, Free,