New Delhi: The coronavirus pandemic has been wreaking havoc all around the world, and has caused more than 27 million infections worldwide, and led to more than 900,000 deaths. As medical experts and researchers are working tirelessly to device an effective, safe, and cheap vaccine against COVID-19, the disease caused due to SARS-CoV-2, or to find a specific and effective cure against the infection, personal and respiratory hygiene and social distancing have been recommended as the only ways of prevention of the disease.

As scientists inch closer to finding ways to treat and prevent the infection, researchers have now found that computer-designed small proteins have now been shown to protect lab-grown human cells from the coronavirus. 

According to a report in Science, in the experiments, it was found that the lead antiviral candidate, named LCB1, known as the best-known coronavirus neutralizing antibodies in its protective actions. The antiviral candidate LCB1 is currently being evaluated in rodents. 

When one looks at the structure of the novel coronavirus, it is observed that the virus is studded with spike protein. These spike proteins are what latch on to human cells, and enable the virus to break in, and infect them. The development of the drugs that interfere with this entry mechanism, according to researchers, can, therefore, help in preventing or treating the infection. 

Researchers from The Institute for Protein Design at the University of Washington School of Medicine used computers to originate new proteins that bind tightly to the virus protein and obstruct it from infecting human cells. 

The study commenced in January. More than 2 million candidate spike-binding proteins have been designed on the computer as yet, and over 118,000 were produced and tested in labs. 

These antiviral proteins were created using two approaches. First, a segment of the ACE2 receptor, the entry point of SARS-CoV-2 in the body was incorporated into a series of small proteins. Another way to do this was to completely synthesise proteins from scratch. The second method had better effects, as it produced more potent antiviral candidates. These were almost six times more potent on a per mass basis than the most effective monoclonal antibodies that have been reported so far. 

The study was conducted by scientists from the Washington School of Medicine in Seattle, in collaboration with the Washington University School of Medicine in St. Louis. 

“Our success in designing high-affinity antiviral proteins from scratch is further proof that computational protein design can be used to create promising drug candidates,” said senior author and Howard Hughes Medical Institute Investigator David Baker, professor of biochemistry at the UW School of Medicine and head of the Institute for Protein Design. 

These experiments were performed by researchers in the laboratories of David Veesler, assistant professor of biochemistry at the UW School of Medicine, and Michael S. Diamond, the Herbert S. Gasser Professor in the Division of Infectious Diseases at Washington University School of Medicine in St. Louis.

“The hyperstable minibinders provide promising starting points for new SARS-CoV-2 therapeutics,” the antiviral research team wrote in their study pre-print, “and illustrate the power of computational protein design for rapidly generating potential therapeutic candidates against pandemic threats.”