The new SARS-CoV-2 strain shows a stronger binding affinity to ACE2due to N501Y mutant
| Autor: | Muhamed Amin, Amal Kasry, Fedaa Ali |
|---|---|
| Přispěvatelé: | Department of Sciences |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
viruses
Mutant Binding energy Molecular dynamics Pharmacy and materia medica Drug Discovery Pharmacology (medical) skin and connective tissue diseases Monte Carlo Pharmacology Electrostatic interactions Strain (chemistry) Chemistry Hydrogen bond SARS-CoV-2 fungi Wild type SARS-CoV Electrostatics Binding domains RS1-441 body regions Mutation (genetic algorithm) Biophysics hormones hormone substitutes and hormone antagonists Research Paper |
| Zdroj: | Medicine in Drug Discovery, 10:100086. Elsevier Medicine in Drug Discovery, Vol 10, Iss, Pp 100086-(2021) Medicine in Drug Discovery |
| ISSN: | 2590-0986 |
| Popis: | SARS-CoV-2 is a global challenge due to its ability to spread much faster than the SARS-CoV, which was attributed to the mutations in the receptor binding domain (RBD). These mutations enhanced the electrostatic interactions. Recently, a new strain is reported in the UK that includes a mutation (N501Y) in the RBD, that is possibly increasing the infection rate. Here, using Molecular Dynamics simulations (MD) and Monte Carlo (MC) sampling, we show that the N501 mutation enhanced the electrostatic interactions due to the formation of a strong hydrogen bond between SARS-CoV-2-T500 and ACE2-D355 near the mutation site. In addition, we observed that the electrostatic interactions between the SARS-CoV-2 and ACE2 in the wild type and the mutant are dominated by salt-bridges formed between SARS-CoV-2-K417 and ACE2-D30, SARS-CoV-2-K458, ACE2-E23, and SARS-CoV-2-R403 and ACE2-E37. These interactions contributed more than 40% of the total binding energies. Graphical abstract Unlabelled Image |
| Databáze: | OpenAIRE |
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