This article has been reviewed according to Science X's editorial process and policies. Editors have highlighted the following attributes while ensuring the content's credibility: Researchers have created a molecular "cage" that keeps protein-degrading drug molecules inactive until they are exposed to low-energy red light. The technology, called RuPHOTACs, controls when and where these molecules become active, which could help scientists develop treatments that destroy specific proteins while limiting unwanted effects elsewhere.
The paper is published in the journal Nature Communications. Protein-degrading technology represents a potentially transformative approach to drug therapies. PROTACs, or PROteolysis-TArgeting Chimeras, work by simultaneously binding to a protein of interest and an enzyme that "tags" that protein for degradation via the natural waste removal processes within cells.
These molecules are dubbed "chimeras" because they bind to and bring together two components: the disease-associated protein and the tag-applying enzyme. As soon as it is finished marking one protein for destruction, it finds another partner and binds, resulting in a much stronger sustained effect. With a PROTAC, you're not just inhibiting the cancer-driving protein; you're removing it," said Edith C. (Phoebe) Glazer, professor of chemistry at North Carolina State University and corresponding author of the study.
However, the main limitation of PROTACs is their effect on surrounding tissue. Many proteins that contribute to cancer and other diseases perform important functions in healthy cells, too. A drug that destroys these proteins throughout the body could cause unwanted side effects.
"Let's say you're focused on cancer treatment," Glazer said. "The problem is there are very few targets—like aberrant proteins—that are only found in cancer. Most of the time, the proteins are important for our healthy tissues too.
So we need a 'cage'; that is, a way to control when and where these PROTACs are activated." Glazer and her colleagues called the cage they developed a RuPHOTAC, or Ruthenium-based PHOToActivated Chimera. Ruthenium, a metal in the platinum group of the periodic table, has properties that make it useful in light-driven processes and chemical reactions. By carefully designing the ruthenium complex, the researchers created a molecular cage that responds to relatively low-energy red light, which penetrates biological tissue effectively.
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