New-type of small molecule switch can control the activity of proteins

According to recent report of the American University of Pittsburgh website, the school research team developed a new technology that using small molecule phosphine as a "switch" to control the activity of the protein. The technology was developed using various recombinant proteins such as recombinant mouse proteins, and it provides a powerful tool for people to better study the biological processes of molecular behavior.

Protein is a kind of elements with the most species in vivo, and it is also one of the most important elements. The growth of teeth, bones, skin and organs and the generation of enzymes and hormones all are inseparable from the proteins. But for living cells which have been completely specialized, the use of proteins varies, and the way of interaction among the systems is different. For scientists, it is a great challenge to determine how they work.

Protein is consisting of long chains of amino acids. In the experiment, the researchers applied a non-natural amino acid in a particular position of certain proteins to make them lose activity, which is called "protection". When they treated the cells with a phosphine reagent to make them to express "protected" proteins, unnatural amino acids could be converted back to natural amino acids, which were out of protection back to active natural type proteins.

The research team used the small molecular switch in relevant processes of four kinds of cells: opening the luciferase activity to trigger cell bioluminescence; activating a protein initially found in jellyfish to cause enhance of fluorescence reaction and converting blue light into green; In the process of protein translocation, they used the small molecular switch to assist proteins to move among cells; In gene editing and DNA recombination, they used the switch to control the insertion and removal of genetic information.

This technology allows researchers to observe the activities of the protein and also helps protein separate from cellular activities. It helps researchers better understand their role and the interaction relationship between it and other ingredients components.

Chemistry Professor Alexander Dai Tesi of the school said that using a drug-like small molecule as external trigger to precisely control the cell-specific protein functions contributes to revealing the activities related to a single protein. A switch which can rapidly activate proteins allows us to learn more about their behavior and function."

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