UC Riverside’s Groundbreaking Approach to Subdue MYC Proteins in 75% of Cancers

Researchers at the University of California – Riverside (UCR) have “tamed” the chaotic MYC proteins that promote and aggravate 75% of cancers. Their work, published in the Journal of the American Chemical Society, suggests a way to control the harmful effects of these proteins, paving the way for more effective anti-cancer drugs.

Cancer News

Cancer News

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The Challenge of Targeting MYC Proteins

In healthy cells, MYC is a critical transcription factor that helps control the process of transcription, in which genetic information is converted from DNA into RNA and finally into proteins. Normally, this MYC activity is strictly controlled. But in cancer cells, MYC becomes overactive and is no longer regulated,” explains lead author Min Xue, Associate Professor of Chemistry at UCR. MYC is thus responsible for aggravating most human cancers. In a wide range of cancers, MYC proteins bind to cell DNA and promote cancer development. The UCR researchers propose a molecule that binds to MYC proteins and thus inhibits their harmful function.

Hope for new  treatments

The study therefore sought to attenuate the hyperactivity of MYC in order to better control the development of cancer. However finding a way to control MYC was a challenge because, unlike most other proteins, MYC has no structure. “It’s basically a random protein. Drug development lines depend on well-defined structures and there is no such structure for MYC.

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Innovative Approach to Taming MYC

In 2018,  the team had already noticed that altering the rigidity and shape of a peptide improved the peptide’s ability to interact with structureless protein targets like MYC. This is because peptides can take on different shapes and positions, making it easier for them to bind to other types of targets.

Development of a New Peptide

The new peptide described here binds directly to the MYC protein with the same strength as an antibody. This interaction is therefore very strong and specific.

Delivery Mechanism and Future Research

The researchers used lipid nanoparticles to introduce the peptide into cells. These are small spheres of fat molecules that are not ideal for use as medicines. The researchers are therefore still working on improving the peptide’s ability to enter the target cells. Once inside the cell, the peptide will bind to the MYC protein, altering its physical properties and preventing it from carrying out harmful transcription activities.

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Implications for Cancer Treatment

The research falls within the field of the chemistry of chaotic processes, where one of the aims is to tame proteins with no specific structure. This has a direct impact on many cancers and promises a new era of treatments.

Final Thoughts

This research could be a game-changer for treating aggressive cancers like lung or breast cancer by offering more targeted, effective treatments. Beyond cancer, the approach may inspire new treatments for other diseases involving protein targeting, signaling a significant advance in personalized medicine and drug development.

References

Li, Z., Huang, Y., Hung, T. I., Sun, J., Aispuro, D., Chen, B., Guevara, N., Ji, F., Cong, X., Zhu, L., Wang, S., Guo, Z., Chang, C.-e., & Xue, M. (2024). MYC-Targeting Inhibitors Generated from a Stereodiversified Bicyclic Peptide Library. Journal of the American Chemical Society, 146(2), 1356–1363. https://doi.org/10.1021/jacs.3c09615

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