Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) undergoes mutations at a high rate and with frequent genetic reassortment (antigenic drift/shift), leading to variability in targets. The receptor-binding domain (RBD) of the spike (S) protein has a major role in the binding of SARS-CoV-2 with human angiotensin-converting enzyme 2 (ACE2). Mutations at the RBD influence the binding interaction at the SARS-CoV-2 S-ACE2 interface and impact viral pathogenicity. Here, we discuss different reported mutations of concern in RBD, physicochemical characteristic changes resulting from mutated amino acids and their effect on binding between the RBD and ACE2. Along with mutation informatics, we highlight recently developed small-molecule inhibitors of RBD and the ACE2 interface. This information provides a rational basis for the design of inhibitors against the multivariant strains of SARS-CoV-2.
Keywords: COVID-19; Entry inhibitors; Mutation informatics; RBD; SARS-CoV-2 variants; Spike protein.
【저자키워드】 COVID-19, spike protein., SARS-CoV-2 variants, RBD, entry inhibitors, Mutation informatics, 【초록키워드】 SARS-CoV-2, ACE2, coronavirus, Mutation, spike, Genetic, Protein, targets, inhibitor, information, characteristic, change, binding, Amino acid, strain, acute respiratory syndrome, antigenic, domain, Variability, human Angiotensin-converting enzyme, viral pathogenicity, highlight, binding interaction, resulting, reported, provide, the RBD, mutated, physicochemical, the SARS-CoV-2, 【제목키워드】 SARS-CoV-2, domain, the spike protein,