About: A hydrophobic-interaction-based mechanism trigger docking between the SARS CoV 2 spike and angiotensin-converting enzyme 2

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About: A hydrophobic-interaction-based mechanism trigger docking between the SARS CoV 2 spike and angiotensin-converting enzyme 2 Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	A hydrophobic-interaction-based mechanism trigger docking between the SARS CoV 2 spike and angiotensin-converting enzyme 2
Creator	Yang, Lin Ye, Lin Guo, Shuai He, Xiaodong Hou, Chengyu Li, Jiacheng Liao, Chencheng Ma, Xiaoliang Shi, Liping Zhang, Hongchi Zheng, Bing
source	ArXiv
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 spike (S) protein of novel severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is more than 10-fold 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 physical mechanism responsible for the outstanding affinity between the SARS-CoV-2 S and ACE2 is the%22urgent challenge%22for developing blockers, vaccines and therapeutic antibodies against the coronavirus disease 2019 (COVID-19) pandemic. Considering 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. We propose a method to design live attenuated viruses by mutating several key amino acid residues of the spike protein to decrease the hydrophobic surface areas at the docking site. Mutation of a small amount of residues can greatly reduce the hydrophobic binding of the coronavirus to the receptor, which may be significant reduce infectivity and transmissibility of the virus.
has issue date	2020-08-27(xsd:dateTime)
has license	arxiv
sha1sum (hex)	6a9942a63f12c3e34c685e883471c9daa11c4604
resource representing a document's title	A hydrophobic-interaction-based mechanism trigger docking between the SARS CoV 2 spike and angiotensin-converting enzyme 2
resource representing a document's body	covid:6a9942a63f12c3e34c685e883471c9daa11c4604#body_text
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