Cell-free protein manufacturing platform a game-changer

New York, Sep 13 (IANS) A team of researchers has developed a user-friendly technology to help scientists understand how proteins work and fix them when they are broken.

The human body has a novel way of turning its proteins on and off to alter their function and activity in cells called phosphorylation — the reversible attachment of phosphate groups to proteins.

Using a special strain of E coli bacteria, the researchers built a cell-free protein synthesis platform technology that can manufacture large quantities of these human phosphoproteins for scientific study.

This will enable scientists to learn more about the function and structure of phosphoproteins and identify which ones are involved in disease.

Such knowledge could pave the way for new drugs for a myriad of diseases, including cancer.

“This innovation will help advance the understanding of human biochemistry and physiology,” said Michael C. Jewett, biochemical engineer from Northwestern University.

Trouble in the phosphorylation process can be a hallmark of disease, such as cancer, inflammation and Alzheimer’s disease.

The human proteome (the entire set of expressed proteins) is estimated to be phosphorylated at more than 100,000 unique sites, making study of phosphorylated proteins and their role in disease a daunting task.

“We now can make these special proteins at unprecedented yields, with a freedom of design that is not possible in living organisms. The consequence of this innovative strategy is enormous,” Jewett pointed out in a paper published in the journal Nature Communications.

Along with Yale University researchers, Jewett combined state-of-the-art genome engineering tools and engineered biological “parts” into a “plug-and-play” protein expression platform that is cell-free.

Cell-free systems activate complex biological systems without using living intact cells.

“Here we are finding new ways to leverage this machinery to understand fundamental biological questions, specifically protein phosphorylation,” Jewett said.

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