The spike (S) protein of coronavirus is the main target for the development of vaccines and a potential strategy to counteract viral entry into human cells. The S protein forms a trimer at the protrusion of the virus and consists of two functional subunits: S1 and S2 [1]. The coronavirus spike protein has been shown to be a multifunctional molecular machine that mediates the entry of coronaviruses into host cells. It first binds to a receptor on the host cell surface through via S1 subunit and then fuses viral and host membranes via its S2 subunit [2]. The receptor-binding domain (RBD) in the S protein is the most flexible part of the coronavirus structure. It has the function of enabling coronaviruses to bind to target body receptors (e.g. ACE2 on respiratory epithelial cells) and enter the cell to cause infection. Thus, blocking the interaction between ACE2 and RBD significantly inhibits viral infection.