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"Chaotic" protein that fuels 75% of all cancers can be controlled with new therapy

In a significant breakthrough, scientists at the University of California, Riverside (UCR) have developed a method to control a notoriously elusive protein called MYC, implicated in 75% of human cancers. This development could ultimately lead to a new era of potential cancer treatments.

MYC’s role in cancer

MYC is a protein that plays a crucial role in the normal functioning of cells, particularly in the transcription process where genetic information transits from DNA to RNA and eventually into proteins. However, in cancer cells, MYC’s activity becomes hyperactive and unregulated.

Fuel for cancer growth 

“Normally, MYC’s activity is strictly controlled. In cancer cells, it becomes hyperactive, and is not regulated properly,” said Professor Min Xue. 

“MYC is less like food for cancer cells and more like a steroid that promotes cancer’s rapid growth. That is why MYC is a culprit in 75% of all human cancer cases.”

A challenging target 

One of the primary challenges in targeting MYC lies in its structure, or lack thereof. MYC’s structureless nature makes it a difficult target for conventional drug discovery methods, which typically rely on well-defined protein structures.

“It’s basically a glob of randomness,” said Professor Xue. “Conventional drug discovery pipelines rely on well-defined structures, and this does not exist for MYC.”

Taming MYC

The UCR team’s innovative approach involved developing a peptide compound that effectively binds to and suppresses MYC’s activity. This was based on their 2018 observation that modifying the rigidity and shape of peptides could enhance their interaction with structureless proteins like MYC. 

By manipulating peptides into specific forms and shapes, the researchers were able to significantly reduce the randomness, facilitating stronger binding to MYC.

Promising results 

The newly developed peptide demonstrates what is known as sub-micro-molar affinity, indicating a strong and specific interaction akin to that of an antibody. This advancement represents a significant leap in binding performance, bringing the research closer to drug development goals. 

“We improved the binding performance of this peptide over previous versions by two orders of magnitude,” said Professor Xue. “This makes it closer to our drug development goals.”

The current phase involves using lipid nanoparticles for peptide delivery into cells, though the team is actively working on improving the peptide’s cell penetration capabilities.

Research funding

This groundbreaking research has been made possible with funding from the U.S. Department of Defense, congressionally directed medical research, and the National Institutes of Health

The implications are profound, potentially paving the way for new, more effective cancer treatments.

Study implications 

Professor Xue, whose lab at UC Riverside is dedicated to developing molecular tools for better understanding biology and drug discovery, is particularly drawn to the chemistry of chaotic processes. He views MYC as embodying chaos due to its lack of structure and its significant impact on various cancer types, making it a prime target in cancer drug development.

As the scientific community eagerly awaits further developments, there is a sense of optimism and excitement. The taming of MYC, once a daunting challenge, is now seemingly within reach, opening new frontiers in the fight against cancer.

“MYC represents chaos, basically, because it lacks structure. That, and its direct impact on so many types of cancer make it one of the holy grails of cancer drug development,” said Professor Xue. “We are very excited that it is now within our grasp.”

The study is published in the Journal of the American Chemical Society.

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