The simulation provides an explanation for SARS-CoV-2 virulence and a potential roadmap for developing tools to disable the virus and future mutated versions. The simulations showed that the spike protein has evolved to be a near perfect fit for the angiotensin-converting enzyme 2 (ACE2) receptor. The precise fit is what ensures that the virus can almost always successfully infect target cells in the human respiratory tract. The simulations also showed the precise shape of the receptor-binding domain region of the spike protein.

The simulations modeled interactions between the spike protein and the receptor for 2 msec. This provided scientists with a view that is approximately 10,000 times longer than most previous simulations. The researchers established a roadmap for the creation of molecules that mimic ACE2 in the body. The simulations also provided key information that can be used to create therapies that change the shape of the receptor-binding domain region to block binding to the receptor.

Microsoft and NantWorks provided the computing resources for the simulation, which provided detailed views of the most likely conformation of the spike protein. The manuscript and a video detailing the findings of the ImmunityBio molecular dynamic simulation studies were published on bioRxiv and is concurrently undergoing scientific peer-review for publication.