Using computational models of protein interactions, researchers at the Massachusetts Institute of Technology (MIT) have developed a peptide that can bind to coronavirus proteins and transfer them to the cell pathway that breaks them down. Researchers have argued that this type of peptide can be used for treatments that prevent the SARS-CoV-2 virus from multiplying in infected cells.

Scientists are pursuing many different strategies to develop new therapeutic agents against SARS-CoV-2. One of the areas of interest is the development of antibodies that bind and deactivate viral proteins. In particular, those that coronavirus uses to enter human cells. Researchers suggested using small protein fragments called peptides instead of antibodies.

The idea of ​​scientists was to use computational methods to develop a peptide that can be a therapeutic agent for COVID-19. Once the peptide enters the cell, it can simply tag and decompose the virus.

To create peptides that bind spike protein, the researchers took a computational model of protein interactions. She was previously trained to optimize the binding strength between two proteins.

As a starting point, scientists used the human protein ACE2 – it is found on the surface of certain types of human cells and binds to the spike protein of the coronavirus.

The researchers used their model to break down ACE2 into many small fragments, and then calculate how these fragments will interact with the adhesive protein.

Scientists have instructed the model to optimize three functions: first, they have developed peptides that can bind to an adhesive protein. Secondly, it was found that peptides can bind well to other proteins of the SARS-CoV2 thorn. Scientists hope peptides will work against past and future strains of coronavirus. Third, they ensured that the peptides would not bind strongly to human proteins.

As a result of this process, about 25 candidate peptides were obtained. Researchers tested them in human cells that expressed a thorn protein fragment known as the receptor binding domain (RBD).

The best of these candidates, a 23-amino acid peptide, cleaves about 20% of RBD proteins in cells.

Researchers are currently planning to test the peptide in human cells infected with the SARS-CoV-2 virus, which will be conducted in specialized biosafety laboratories outside of MIT. If these tests succeed, scientists hope to test the peptide in animal models. They are also working to further improve the peptide so that it can more strongly bind the spike protein.