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A recent experimental study found that the binding affinity between thecellular receptor human angiotensin converting enzyme 2 (ACE2) andreceptor-binding domain (RBD) in spike (S) protein of novel severe acuterespiratory syndrome coronavirus 2 (SARS-CoV-2) is more than 10-fold higherthan that of the original severe acute respiratory syndrome coronavirus(SARS-CoV). However, main-chain structures of the SARS-CoV-2 RBD are almost thesame with that of the SARS-CoV RBD. Understanding physical mechanismresponsible for the outstanding affinity between the SARS-CoV-2 S and ACE2 isthe "urgent challenge" for developing blockers, vaccines and therapeuticantibodies against the coronavirus disease 2019 (COVID-19) pandemic.Considering the mechanisms of hydrophobic interaction, hydration shell, surfacetension, and the shielding effect of water molecules, this study reveals ahydrophobic-interaction-based mechanism by means of which SARS-CoV-2 S and ACE2bind together in an aqueous environment. The hydrophobic interaction betweenthe SARS-CoV-2 S and ACE2 protein is found to be significantly greater thanthat between SARS-CoV S and ACE2. At the docking site, the hydrophobic portionsof the hydrophilic side chains of SARS-CoV-2 S are found to be involved in thehydrophobic interaction between SARS-CoV-2 S and ACE2. We propose a method todesign live attenuated viruses by mutating several key amino acid residues ofthe spike protein to decrease the hydrophobic surface areas at the dockingsite. Mutation of a small amount of residues can greatly reduce the hydrophobicbinding of the coronavirus to the receptor, which may be significant reduceinfectivity and transmissibility of the virus.

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