Groundbreaking Discovery: Peptide Controls Key Protein in Cancer Cells, Paving the Way for More Effective Treatment
In a groundbreaking discovery, researchers at the University of California, Riverside (UCR) have developed a peptide that can control MYC, a key protein involved in the majority of human cancers. This innovative breakthrough offers new hope for targeting cancer at a molecular level, potentially leading to more effective treatments.
MYC, the shapeless protein responsible for exacerbating the majority of human cancer cases, has long been a challenge for researchers. In healthy cells, MYC plays a role in guiding the process of transcription, converting genetic information from DNA into RNA and eventually proteins. However, in cancer cells, MYC becomes hyperactive and loses its proper regulation.
According to UCR associate professor of chemistry, Min Xue, “MYC is less like food for cancer cells and more like a steroid that promotes cancer’s rapid growth.” This explains why MYC is implicated in 75% of all human cancer cases. The UCR research team believed that if they could dampen MYC’s hyperactivity, they could potentially control cancer growth.
Controlling MYC proved challenging due to its lack of structure compared to other proteins. Xue describes it as “basically a glob of randomness.” Conventional drug discovery pipelines rely on well-defined structures, which do not exist for MYC. However, the researchers took an innovative approach to drug discovery.
Their findings, published in the Journal of the American Chemical Society, detail the development of a peptide compound that binds to MYC and suppresses its activity. The researchers discovered that by changing the rigidity and shape of the peptide, they could enhance its ability to interact with structureless proteins like MYC.
“Peptides can assume a variety of forms, shapes, and positions,” explains Xue. “Once you bend and connect them to form rings, they cannot adopt other possible forms, so they then have a low level of randomness. This helps with the binding.”
The team successfully developed a peptide that binds directly to MYC with sub-micro-molar affinity, approaching the strength of an antibody. This strong and specific interaction marks a significant improvement over previous versions of the peptide.
Currently, the researchers are exploring the use of lipid nanoparticles to deliver the peptide into cells. While lipid nanoparticles are not ideal for use as a drug, they serve as a starting point for further development. The team is working on enhancing the peptide’s ability to enter cells through improved chemistry.
Once inside the cell, the peptide will bind to MYC, altering its physical properties and preventing it from performing transcription activities. This breakthrough has been made possible through funding from the U.S. Department of Defense, congressionally directed medical research, and the National Institutes of Health.
Min Xue’s laboratory at UC Riverside focuses on developing molecular tools to better understand biology and utilize that knowledge for drug discovery. Xue has been particularly interested in chaotic processes, which led him to tackle the challenge of taming MYC.
“MYC represents chaos because it lacks structure,” says Xue. “That, combined with its direct impact on various types of cancer, makes it one of the holy grails of cancer drug development. We are very excited that it is now within our grasp.”
This groundbreaking discovery opens up new possibilities for cancer treatment by targeting MYC, a protein that plays a significant role in cancer progression. With further development and refinement, this peptide-based approach could lead to more effective treatments and bring hope to millions of cancer patients worldwide.
