Revolutionizing Antibiotics: How MIT’s Water-Soluble Enzymes Could Change the Game

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Researchers at MIT have developed a water-soluble version of the bacterial enzyme histidine kinase, which is a promising target for new antibiotics due to its unique presence in bacteria. The modified enzyme retains its natural functions and could be crucial in combating antibiotic resistance, which claims over a million lives annually. Credit: SciTechDaily.com

“Each year, more than 1 million people die from antibiotic-resistant infections,” says Shuguang Zhang, a principal research scientist in the MIT Media Lab and one of the senior authors of the new study. “This protein is a good target because it’s unique to bacteria and humans don’t have it.” Since then, the researchers have demonstrated this technique on a variety of hydrophobic proteins, including antibodies, cytokine receptors, and transporters. Those transporters include a protein that cancer cells use to pump chemotherapy drugs out of the cells, as well as transporters that brain cells use to move dopamine and serotonin into or out of cells.

Histidine kinase can perform four different functions, including phosphorylation and dephosphorylation . Human cells also have kinases, but they act on amino acids other than histidine, so drugs that block histidine kinase would likely not have any effect on human cells. “If we can use the same tool, the QTY code, on methane monooxygenase, and use that enzyme to convert methane into methanol, that could deaccelerate climate change,” Zhang says.

 

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