ArticleMolecular diversity2022
Computational prediction of the effect of mutations in the receptor-binding domain on the interaction between SARS-CoV-2 and human ACE2.
Article in Molecular diversity, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 32 citations in OpenAlex.
- A multi-epitope pan-betacoronavirus vaccine construct predicted to induce broad-spectrum and durable immune responses: an immunoinformatics approach.Frontiers in bioinformatics · 2026Article
- A network pharmacology approach to elucidate the anti-inflammatory and antioxidant effects of bitter leaf (Narra J · 2024Article
- Structure-guided engineering and molecular simulations to design a potent monoclonal antibody to target aP2 antigen for adaptive immune response instigation against type 2 diabetes.Frontiers in immunology · 2024Article
- A computational simulation appraisal of banana lectin as a potential anti-SARS-CoV-2 candidate by targeting the receptor-binding domain.Journal, genetic engineering & biotechnology · 2023Article
- Low-Entropy Hydration Shells at the Spike RBD's Binding Site May Reveal the Contagiousness of SARS-CoV-2 Variants.Biomolecules · 2023Article
- 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
- Pyrazolo[4,3-International journal of molecular sciences · 2023Article
- Mutational analysis of catalytic site domain of CCHFV L RNA segment.Journal of molecular modeling · 2023Article
- The impact of mutation sets in receptor-binding domain of SARS-CoV-2 variants on the stability of RBD-ACE2 complex.Future virology · 2023Article
- Design of a chimeric ACE-2/Fc-silent fusion protein with ultrahigh affinity and neutralizing capacity for SARS-CoV-2 variants.Antibody therapeutics · 2023Article
- Prediction of infectivity of SARS-CoV2: Mathematical model with analysis of docking simulation for spike proteins and angiotensin-converting enzyme 2.Microbial risk analysis · 2022Article
- Article
- Genomic and structural mechanistic insight to reveal the differential infectivity of omicron and other variants of concern.Computers in biology and medicine · 2022Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) causing COVID-19 continues to mutate. Numerous studies have indicated that this viral mutation, particularly in the receptor-binding domain area, may increase the viral affinity for human angiotensin-converting enzyme 2 (hACE2), the receptor for viral entry into host cells, thereby increasing viral virulence and transmission. In this study, we investigated the binding affinity of SARS-CoV-2 variants (Delta plus, Iota, Kappa, Mu, Lambda, and C.1.2) on hACE2 using computational modeling with a protein-protein docking approach. The simulation results indicated that there were differences in the interactions between the RBD and hACE2, including hydrogen bonding, salt bridge interactions, non-bonded interactions, and binding free energy differences among these variants. Molecular dynamics simulations revealed that mutations in the RBD increase the stability of the hACE2-spike protein complex relative to the wild type, following the global stability trend and increasing the binding affinity. The value of binding-free energy calculated using molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) indicated that all mutations in the spike protein increased the contagiousness of SARS-CoV-2 variants. The findings of this study provide a foundation for developing effective interventions against these variants. Computational modeling elucidates that the spike protein of SARS-CoV-2 variants binds considerably stronger than the wild-type to hACE2.
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