The Myc protein is part of the activity of healthy cells, but as cancer cells grow, it becomes disrupted and loses its normal role of promoting the spread of cancer; Scientists may have found a way to prevent this.
“Normally, Myc activity is tightly controlled. In cancer cells, it becomes overactive and is not regulated properly,” explains biochemist Min Xue.
By successfully curbing Myc activity, researchers hope to find a method that stops one of the ways cancer hijacks healthy biological processes in order to survive.
A complex task
Part of the problem with controlling Myc is that it is an amorphous protein whose structure is not really vulnerable to attack. This makes it difficult for medications to effectively identify Myc and prevent it from behaving normally.
However, a team at the University of California, Riverside (UCR) has managed to develop a peptide compound capable of binding or interacting with Myc and helping it regain control.
The results of their research were published in the Journal of the American Chemical Society.
“Myc is less a food for cancer cells and more a steroid that promotes rapid cancer growth,” says Xue, who works for UCR.
“This is why Myc is the cause of 75% of all human cancers,” he adds.
Mr. Xue says Myc's importance in cancer makes neutralizing its harmful effects one of the “holy grails of cancer drug development.” He adds that he and his colleagues are particularly “thrilled” that such a cure is now within reach.
The researchers were able to examine Myc's small amounts of structure to build a library of peptides that could attach to this structure. One peptide in particular, NT-B2R, has been shown to be particularly effective at deactivating Myc.
NT-B2R successfully binds to myc, thereby changing the way its cells regulate many of their genes, thereby reducing cancer cell metabolism and proliferation.
Previous work
The key to this breakthrough lies in previous work by some of the same researchers, who found that by changing the structure and shape of peptides, these molecules were better able to interact with amorphous proteins like Myc.
“Peptides can take on a wide variety of shapes and positions. Once you bend them and connect them into rings, they cannot take on other possible shapes, giving them a small degree of randomness. This makes bonding easier,” says Xue.
“We have improved the binding performance of this peptide by two orders of magnitude compared to previous versions. “This brings us closer to our drug development goals,” he says.
There is still a lot to do, but the early results are promising.