Ivermectin, a common anti-parasite drug, has shown great efficacy in the fight against covid-19. For the first time, medical researchers have documented how ivermectin docks to the SARS-CoV-2 spike receptor-binding domain that is attached to the ACE2 receptor. In this way, ivermectin effectively inhibits viral attachment and replication, assisting a precise antiviral response that can target the SARS-CoV-2 spike protein at its most advantageous cleavage site. The researchers showed how ivermectin interferes with the attachment of the spike protein to the human cell membrane.

Ivermectin is a simple medicine derived from the bacterium Streptomyces avermitilis. It weakens and kills parasites by interfering with their nervous system and muscle function. Ivermectin targets the glutamate-gated chloride channels in the parasite's nerve and muscle cells, bolstering inhibitory effects in the parasite's own neurotransmission. As the chloride ions permeate, the parasite's cells are hyper-polarized and then paralyzed, resulting in their demise.

In this study, ivermectin docked in region of leucine 91 of the spike protein and at the histidine 378 of the ACE2 receptor. The binding energy and constancy of ivermectin was also measured and found to be sufficient at the ACE2 receptor, proving the anti-parasitic molecule a powerful force for blocking viral attachment of SARS-CoV-2.