The Delta Variant Mutations in the Receptor Binding Domain of SARS-CoV-2 Show Enhanced Electrostatic Interactions with the ACE2.
| Autor: | Goher SS; Nanotechnology Research Centre (NTRC), the British University in Egypt (BUE), El Sherouk City, Suez Desert Road, Cairo 1183, Egypt., Ali F; Department of Sciences, University College Groningen, University of Groningen, Hoendiepskade 23/24, 9718 BG Groningen, The Netherlands., Amin M; Center for Free-Electron Laser Science, Deutsches Elektronen-Synchrotron DESY, Notkestrasse 85, 22607 Hamburg, Germany. |
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| Jazyk: | angličtina |
| Zdroj: | Medicine in drug discovery [Med Drug Discov] 2021 Dec 04, pp. 100114. Date of Electronic Publication: 2021 Dec 04. |
| DOI: | 10.1016/j.medidd.2021.100114 |
| Abstrakt: | Mutations in the receptor binding domain (RBD) in SARS-CoV-2 are shown to enhance its replication, transmissibility, and binding to host cells. Recently, a new strain is reported in India that includes a mutation (T478K, and L452R) in the RBD, that is possibly increasing the infection rate. Here, using Molecular Mechanics (MM) and Monte Carlo (MC) sampling, we show that the double mutant variant of SARS-CoV-2 induced conformational change in ACE2-E37, which enhanced the electrostatic interactions by the formation of a salt-bridge with SARS-CoV-2-R403. In addition, we observed that the double mutated structure induced a significant change in the salt-bridge electrostatic interaction between RBD-T500 and ACE2-D355. Where that this interaction lost more than 70% of its value compared to its value in WT protein. (© 2021 The Author(s).) |
| Databáze: | MEDLINE |
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