{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tang C"],"funding":["Strategic Priority Research Program of the Chinese Academy of Sciences","Guangdong Basic and Applied Basic Research Foundation","National Natural Science Foundation of China","National Key research and development program of China","Shenzhen Science and Technology Program","Research Grants Council of the HKSAR"],"pagination":["3776"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12027596"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["26(8)"],"pubmed_abstract":["The evolution of SARS-CoV-2, particularly the emergence of Omicron variants, has raised questions regarding changes in its binding affinity to the human angiotensin-converting enzyme 2 receptor (hACE2). Understanding the impact of mutations on the interaction between the receptor-binding domain (RBD) of the spike protein and hACE2 is critical for evaluating viral transmissibility, immune evasion, and the efficacy of therapeutic strategies. Here, we used molecular dynamics (MD) simulations and binding energy calculations to investigate the structural and energetic differences between the hACE2- RBD complexes of wild-type (WT), Delta, and Omicron subvariants. Our results indicate that the Delta and the first Omicron variants showed the highest and the second-highest binding energy among the "],"journal":["International journal of molecular sciences"],"pubmed_title":["Structural and Energetic Insights into SARS-CoV-2 Evolution: Analysis of hACE2-RBD Binding in Wild-Type, Delta, and Omicron Subvariants."],"pmcid":["PMC12027596"],"funding_grant_id":["32170672, 32000886","XDB0480000","2021A1515012461","ZDSYS20220606100606013","2021YFA0911100","12304020, 12301723"],"pubmed_authors":["Li X","Wang D","Tang C","Tang LH","Lupala CS"],"additional_accession":[]},"is_claimable":false,"name":"Structural and Energetic Insights into SARS-CoV-2 Evolution: Analysis of hACE2-RBD Binding in Wild-Type, Delta, and Omicron Subvariants.","description":"The evolution of SARS-CoV-2, particularly the emergence of Omicron variants, has raised questions regarding changes in its binding affinity to the human angiotensin-converting enzyme 2 receptor (hACE2). Understanding the impact of mutations on the interaction between the receptor-binding domain (RBD) of the spike protein and hACE2 is critical for evaluating viral transmissibility, immune evasion, and the efficacy of therapeutic strategies. Here, we used molecular dynamics (MD) simulations and binding energy calculations to investigate the structural and energetic differences between the hACE2- RBD complexes of wild-type (WT), Delta, and Omicron subvariants. Our results indicate that the Delta and the first Omicron variants showed the highest and the second-highest binding energy among the ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Apr","modification":"2026-04-08T19:22:07.647Z","creation":"2026-04-08T13:21:08.109Z"},"accession":"S-EPMC12027596","cross_references":{"pubmed":["40332432"],"doi":["10.3390/ijms26083776"]}}