Abstract
The COVID-19 pandemic has become a global health challenge because of the emergence of distinct variants. Omicron, a new variant, is recognized as a variant of concern (VOC) by the World Health Organization (WHO) because of its higher mutations and accelerated human infection. The infection rate is strongly dependent on the binding rate of the receptor binding domain (RBD) against human angiotensin converting enzyme-2 (ACE2 human ) receptor. Inhibition of protein-protein (RBDs (SARS-CoV-2/omicron) -ACE2 human ) interaction has been already proven to inhibit viral infection. We have systematically designed ACE2 human -derived peptides and peptide mimetics that have high binding affinity toward RBD omicron . Our peptide mutational analysis indicated the influence of canonical amino acids on the peptide binding process. Herein, efforts have been made to explore the atomistic details and events of RBDs (SARS-CoV-2/omicron) -ACE2 human interactions by using molecular dynamics simulation. Our studies pave a path for developing therapeutic peptidomimetics against omicron.
【초록키워드】 viral infection, ACE2, Mutation, VoC, COVID-19 pandemic, variant, peptide, molecular dynamics, inhibition, omicron, variants, binding affinity, Molecular dynamics simulation, Receptor binding domain, Angiotensin converting enzyme-2, Health, RBD, therapeutic, peptides, amino acids, WHO, receptor, infection rate, binding, Amino acid, Interaction, Analysis, angiotensin, RBDs, Health Organization, World Health Organization, human infection, effort, path, event, indicated, inhibit, dependent on, accelerated, canonical, 【제목키워드】 SARS-CoV-2, Therapeutics, identification, Potential,