tetano
Editor, Senior Moderator
Glob Chall
. 2020 Oct 15;2000067.
doi: 10.1002/gch2.202000067. Online ahead of print.
A Hydrophobic-Interaction-Based Mechanism Triggers Docking between the SARS-CoV-2 Spike and Angiotensin-Converting Enzyme 2
Jiacheng Li[SUP] 1 [/SUP], Xiaoliang Ma[SUP] 1 [/SUP], Shuai Guo[SUP] 1 [/SUP], Chengyu Hou[SUP] 2 [/SUP], Liping Shi[SUP] 1 [/SUP], Hongchi Zhang[SUP] 1 [/SUP], Bing Zheng[SUP] 3 [/SUP], Chenchen Liao[SUP] 2 [/SUP], Lin Yang[SUP] 1 4 [/SUP], Lin Ye[SUP] 4 [/SUP], Xiaodong He[SUP] 1 5 [/SUP]
Affiliations
Abstract
A recent experimental study found that the binding affinity between the cellular receptor human angiotensin-converting enzyme 2 (ACE2) and receptor-binding domain (RBD) in the spike (S) protein of novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is more than tenfold higher than that of the original severe acute respiratory syndrome coronavirus (SARS-CoV). However, main chain structures of the SARS-CoV-2 RBD are almost the same with that of the SARS-CoV RBD. Understanding the physical mechanism responsible for the outstanding affinity between the SARS-CoV-2 S and ACE2 is an "urgent challenge" for developing blockers, vaccines, and therapeutic antibodies against the coronavirus disease 2019 (COVID-19) pandemic. Taking into account the mechanisms of hydrophobic interaction, hydration shell, surface tension, and the shielding effect of water molecules, this study reveals a hydrophobic-interaction-based mechanism by means of which SARS-CoV-2 S and ACE2 bind together in an aqueous environment. The hydrophobic interaction between the SARS-CoV-2 S and ACE2 protein is found to be significantly greater than that between SARS-CoV S and ACE2. At the docking site, the hydrophobic portions of the hydrophilic side chains of SARS-CoV-2 S are found to be involved in the hydrophobic interaction between SARS-CoV-2 S and ACE2.
Keywords: COVID‐19; SARS‐CoV‐2; angiotensin‐converting enzyme 2; coronavirus; docking; hydrophobic interactions.
. 2020 Oct 15;2000067.
doi: 10.1002/gch2.202000067. Online ahead of print.
A Hydrophobic-Interaction-Based Mechanism Triggers Docking between the SARS-CoV-2 Spike and Angiotensin-Converting Enzyme 2
Jiacheng Li[SUP] 1 [/SUP], Xiaoliang Ma[SUP] 1 [/SUP], Shuai Guo[SUP] 1 [/SUP], Chengyu Hou[SUP] 2 [/SUP], Liping Shi[SUP] 1 [/SUP], Hongchi Zhang[SUP] 1 [/SUP], Bing Zheng[SUP] 3 [/SUP], Chenchen Liao[SUP] 2 [/SUP], Lin Yang[SUP] 1 4 [/SUP], Lin Ye[SUP] 4 [/SUP], Xiaodong He[SUP] 1 5 [/SUP]
Affiliations
- PMID: 33173592
- PMCID: PMC7646041
- DOI: 10.1002/gch2.202000067
Abstract
A recent experimental study found that the binding affinity between the cellular receptor human angiotensin-converting enzyme 2 (ACE2) and receptor-binding domain (RBD) in the spike (S) protein of novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is more than tenfold higher than that of the original severe acute respiratory syndrome coronavirus (SARS-CoV). However, main chain structures of the SARS-CoV-2 RBD are almost the same with that of the SARS-CoV RBD. Understanding the physical mechanism responsible for the outstanding affinity between the SARS-CoV-2 S and ACE2 is an "urgent challenge" for developing blockers, vaccines, and therapeutic antibodies against the coronavirus disease 2019 (COVID-19) pandemic. Taking into account the mechanisms of hydrophobic interaction, hydration shell, surface tension, and the shielding effect of water molecules, this study reveals a hydrophobic-interaction-based mechanism by means of which SARS-CoV-2 S and ACE2 bind together in an aqueous environment. The hydrophobic interaction between the SARS-CoV-2 S and ACE2 protein is found to be significantly greater than that between SARS-CoV S and ACE2. At the docking site, the hydrophobic portions of the hydrophilic side chains of SARS-CoV-2 S are found to be involved in the hydrophobic interaction between SARS-CoV-2 S and ACE2.
Keywords: COVID‐19; SARS‐CoV‐2; angiotensin‐converting enzyme 2; coronavirus; docking; hydrophobic interactions.