Examining the interactions scorpion venom peptides (HP1090, Meucin-13, and Meucin-18) with the receptor binding domain of the coronavirus spike protein to design a mutated therapeutic peptide

The spike protein of SARS-CoV-2 (Severe Acute Respiratory Syndrome coronavirus 2) interacts with the ACE2 receptor in human cells and starts the infection of COVID-19 disease. Given the importance of spike protein's interaction with ACE2 receptor, we selected some antiviral peptides of venom scorpion such as HP1090, meucin-13, and meucin-18 and performed docking and molecular docking analysis of them with the RBD domain of spike protein. The results showed that meucin-18 (FFGHLFKLATKIIPSLFQ) had better interaction with the RBD domain of spike protein than other peptides. We also designed some mutations in meucin-18 and investigated their interactions with the RBD domain. The results revealed that the A9T mutation had more effective interaction with the RBD domain than the meucin-18 and was able to inhibit spike protein's interaction with ACE2 receptor. Hence, peptide “FFGHLFKLTTKIIPSLFQ” can be considered as the potential drug for the treatment of COVID-19 disease.