Although the protein MYC is part of healthy cellular activity, it is normally regulated when cancer cells develop, and it deviates from its carefully regulated role. help spread cancer. Now, scientists may have found a way to stop this.
One of the problems with controlling MYC is that it is an amorphous protein and doesn’t really have a structure that it can target. This makes it difficult for drugs to effectively identify MYC and maintain its normal operation.
However, a team from the University of California, Riverside (UCR) peptide compounds This helps to bind or interact with MYC and bring it back under control.
“Rather than being food for cancer cells, MYC is more like a steroid that promotes rapid cancer growth.” To tell Min Xue, a biochemist from UCR. “That’s why MYC is responsible for 75 percent of all human cancer cases.”
“Normally, MYC activity is tightly regulated. In cancer cells, the activity is increased and not properly regulated.”
By studying the small amount of structure that MYC has, the researchers were able to build a library of peptides that could potentially capture it. One peptide in particular, NT-B2R, proved to be particularly good at disabling MYC.
In studies using cultures made from human brain tumor cells, NT-B2R successfully binds to MYC, changing the way the cell regulates many of its genes and ultimately leading to changes in cancer cells. Shown to reduce metabolism and proliferation. It’s a bit like tying someone’s hands behind their back so they can’t do much.
The key to the breakthrough was previous job Some of the same researchers realized that as the structure and shape of peptides change, these molecules become better able to interact with shapeless proteins like MYC.
“Peptides can take on a variety of shapes, shapes, and positions. Once bent and connected to form a ring, they cannot take on any other possible shape, making them less random. This is due to the binding It helps.” To tell Shue.
“We improved the binding performance of this peptide by two orders of magnitude over previous versions, which brings this peptide closer to our drug development goals.”
Although these early results are promising, there is still much work to be done. Currently, peptides are delivered through fat globules called fat globules. lipid nanoparticlesThis is not very suitable for dispensing medicines and must be changed.
The researchers may have found a way to stop one of the ways cancer hijacks healthy biological processes, although more rigorous testing in humans is still needed. to survive.
“MYC basically represents chaos, because it lacks structure.” To tell Shue.
“It directly impacts so many types of cancer, making it one of the holy grails of cancer drug development. We are very excited that it is now within reach.” Masu.”
This research Journal of the American Chemical Society.