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BGU Research Speeds-up Timeframe Needed to Screen Drugs

BGU Research Speeds-up Timeframe Needed to Screen Drugs

January 24, 2020

Medical Research

The Jerusalem Post — What if drugs for cancer could be developed faster, allowing treatment to be delivered quicker, too? A team of cancer researchers, headed by Ben-Gurion University of the Negev’s Dr. Niv Papo and Hebrew University of Jerusalem Prof. Julia Shifman, are working to do just that.

A joint statement from the two universities explained that with thousands of potential mutations for every protein to protein interaction, “the process [for screening potential treatment drugs] was costly, labor-intensive and time-consuming.”

The team has developed a powerful tool to simultaneously evaluate thousands of mutations in protein to protein complexes and to map their effect on protein binding affinity, turning a process that could take years into one that takes just a few days.

Dr. Niv Papo

“We generate a protein library in which each member of the library carries a single mutation in the protein so that the entire library consists of millions of different protein mutants,” said Dr. Papo of BGU’s Avram and Stella Goldstein-Goren Department of Biotechnology Engineering and the National Institute for Biotechnology in the Negev (NIBN).

He explained that they then screen this protein library against the target protein. This is how they can give a score to each mutant according to its ability to bind and inhibit the target.

“The method allows us to screen millions of such mutations and determine which ones of these mutations affect the affinity of the disease-related protein to its target,” he continued. “Knowing this allows us to develop inhibitors against these specific disease-related protein mutants and also to understand the mechanism of disease progression,” meaning what protein mutations are causing the disease. This means that the timeframe for generating the drug can now be much shorter.

“We can easily and very quickly identify and isolate protein-based drugs that have strong binding affinity and specificity, as well as inhibition potency towards the disease-related target,” he said.

This new method of quantifying the effect of thousands of mutations allows researchers to design protein drugs that are both potent and specific, causing minimal side effects.

Their findings were published in Nature Communications.

Read more on The Jerusalem Post website >>