ArticleBiochemical and biophysical research communications2022
Scanning the RBD-ACE2 molecular interactions in Omicron variant.
Article in Biochemical and biophysical research communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Allosteric effects of CDR-H3 mutations modulate binding and neutralization of a conserved SARS-CoV-2 RBD-targeting antibody.Microbiology spectrum · 2026Article
- Subtle Changes at the RBD/hACE2 Interface During SARS-CoV-2 Variant Evolution: A Molecular Dynamics Study.Biomolecules · 2025Article
- Deep learning for discriminating non-trivial conformational changes in molecular dynamics simulations of SARS-CoV-2 spike-ACE2.Scientific reports · 2024Article
- Three-Dimensional Structural Stability and Local Electrostatic Potential at Point Mutations in Spike Protein of SARS-CoV-2 Coronavirus.International journal of molecular sciences · 2024Article
- SARS-CoV-2 omicron spike simulations: broad antibody escape, weakened ACE2 binding, and modest furin cleavage.Microbiology spectrum · 2023Article
- Article
- Comparative Study of the Mutations Observed in the SARS-CoV-2 RBD Variants of Concern and Their Impact on the Interaction with the ACE2 Protein.The journal of physical chemistry. B · 2023Article
- Identification of inhibitors against SARS-CoV-2 variants of concern using virtual screening and metadynamics-based enhanced sampling.Chemical physics · 2023Article
- Omicron Coronavirus: pH-Dependent Electrostatic Potential and Energy of Association of Spike Protein to ACE2 Receptor.Viruses · 2023Article
- Different In Silico Approaches Using Heterocyclic Derivatives against the Binding between Different Lineages of SARS-CoV-2 and ACE2.Molecules (Basel, Switzerland) · 2023Article
- Deep Structural Analysis of Myriads of Omicron Sub-Variants Revealed Hotspot for Vaccine Escape Immunity.Vaccines · 2023Article
- RNA loads of severe acute respiratory syndrome coronavirus 2 in patients with breakthrough coronavirus disease 2019 caused by the Delta and Omicron variants.Clinical microbiology and infection : the official publication of the European Society of Clinical Microbiology and Infectious Diseases · 2023Observational
- Bionics design of affinity peptide inhibitors for SARS-CoV-2 RBD to block SARS-CoV-2 RBD-ACE2 interactions.Heliyon · 2023Article
- The outbreak of SARS-CoV-2 Omicron lineages, immune escape, and vaccine effectivity.Journal of medical virology · 2023Review
- Reversal of the unique Q493R mutation increases the affinity of Omicron S1-RBD for ACE2.Computational and structural biotechnology journal · 2023Article
- SARS-CoV-2 and its impact on the cardiovascular and digestive systems - The interplay between new virus variants and human cells.Computational and structural biotechnology journal · 2023Review
- Conformational Dynamics of the Receptor-Binding Domain of the SARS-CoV-2 Spike Protein.Biomedicines · 2022Article
- Omicron BA.1 and BA.2 variants increase the interactions of SARS-CoV-2 spike glycoprotein with ACE2.Journal of molecular graphics & modelling · 2022Article
- Structural Profiles of SARS-CoV-2 Variants in India.Current microbiology · 2022Article
- Evolutionary trajectory of receptor binding specificity and promiscuity of the spike protein of SARS-CoV-2.Protein science : a publication of the Protein Society · 2022Article
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3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The emergence of new SARS-CoV-2 variants poses a threat to the human population where it is difficult to assess the severity of a particular variant of the virus. Spike protein and specifically its receptor binding domain (RBD) which makes direct interaction with the ACE2 receptor of the human has shown prominent amino acid substitutions in most of the Variants of Concern. Here, by using all-atom molecular dynamics simulations we compare the interaction of Wild-type RBD/ACE2 receptor complex with that of the latest Omicron variant of the virus. We observed a very interesting diversification of the charge, dynamics and energetics of the protein complex formed upon mutations. These results would help us in understanding the molecular basis of binding of the Omicron variant with that of SARS-CoV-2 Wild-type.
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