PNAS: Receptor binding of SARS-CoV-2 is enhanced through hydrogen bond and hydrophobic interaction.

, June 28, 2020 //bio-valleyBIOON/-- Severe Acute Respiratory Syndrome Type 2 coronavirus (SARS-CoV-2) enhanced receptor binding is thought to be the cause of the highly contagious transmission rate of coronavirus disease in 2019Understanding the structure and energy details of the protein-protein interactionbetween host receptors ACE2 and SARS-CoV-2 can help with outbreak surveillance,diagnosis
and the optimization of neutralisive agentsto clarify the structural sources of different protein-protein interactions between the receptor binding regions of SARS-CoV and SARS-CoV-2, from the Institute of Systems and Physical Biology of Shenzhen Bay Laboratory, the School of Chemical Biology and Biotechnology of The Shenzhen Graduate School of Peking University, Researchers from the Department of Chemistry at the University of Minnesota and the University of Minnesota's Institute of Supercomputing Technology conducted simulations of lung molecular dynamics and free energy, published recently in PNAS, entitled "Enhanced weight binding of SARS-CoV-2 through hydrogen-boding and hydrophopho interactions"image source: PNASdynamic trajectory analysis results show that in the 2019 new coronavirus, the interface between ACE2 and receptor binding domain is mainly composed of hydrophobic areas and fine hydrogen bond networksThe researchers found that a key mutation was a hydrophobic residue mutation corresponding to LYs417 in SARS-CoV-2, which led to the formation of a salt bridge in the hydrophobic contact regional center, which, together with the polar residue mutation, resulted in greater electrostatic complementarity than the SARS-CoV complexin addition, the researchers found that the electrostatic effect and enhanced hydrophobic regions (removing 4 of the five proline residues in 12 short residual rings) caused the SARS-CoV-2 complex to dowx to shift toward skewed junctions compared to the SARS-CoV complexon the other hand, the researchers found that in the SARS-CoV-2 homologous complex model, hydrophobic contact in THE SARS-CoV-2 and the antibody 80R complex was destroyed, due to the inability of 80R to recognize SARS-CoV-2overall, in this study, using molecular dynamics to simulate the RBD domain of SARS and COVID-19 viruses with the binary compounds of common receptors ACE2 and antibody 80R, the researchers found that electrostatic complementarity and hydrophobic interactions were essential for enhancing the receptor binding and evasion of antibody recognition in SARS-CoV-2(BioValleyBioon.com)References:Yingjie Wang et alEnhanced oedd ei binding of SARS-CoV-2 through the networks of hydrogen-bonding and hydrophobic interactions PNAS June 23, 2020 117 (25) 13967-13974; firstpublished June 5, 2020 https://doi.org/10.1073/pnas.2008209117
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