The protein MYC is involved in normal cell activity, but as cancer cells grow, it goes haywire, deviating from its typical, tightly regulated function and promoting the growth of cancer. Scientists are trying to figure out how to prevent this from happening.
The fact that MYC is a shapeless protein with no actual targetable structure contributes to the difficulty in controlling it. This makes it challenging for medications to recognize MYC and maintain its proper behavior.
A group at the University of California, Riverside (UCR) has created a peptide compound that interacts or binds with MYC and assists in bringing it under control again.
“MYC is less like food for cancer cells and more like a steroid that promotes cancer’s rapid growth,” says biochemist Min Xue, from UCR. “That is why MYC is a culprit in 75 percent of all human cancer cases.”
By examining the little structure that MYC does have, the researchers were able to compile a library of peptides that may be able to attach themselves to that structure. NT-B2R was one peptide in particular that showed exceptional skill at blocking MYC.
NT-B2R was demonstrated to attach to MYC with success in experiments conducted on a culture of human brain cancer cells. This alteration in gene regulation of MYC led to a reduction in the cancer cells’ proliferation and metabolism. It prevents them from doing anything at all, much like tying their hands behind their back.
A prior study by some of the same scientists, which found that altering the structure and form of peptides improved their ability to interact with shapeless proteins like MYC, was crucial to the discovery.
“Peptides can assume a variety of forms, shapes, and positions. 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,” says Xue. He also stated that they achieved a two-fold increase in binding performance over the prior iteration of this peptide. This helped them to achieve their drug development objectives.
These preliminary findings are encouraging, but much work remains. It will be necessary to alter the current method of delivering the peptide, which involves using lipid nanoparticles, which are fatty spheres unsuitable for medication distribution.
Thorough experiments on humans will also need to be conducted, but perhaps we have discovered a technique to block one of the ways cancers uses normal biological functions as a means of survival.
“MYC represents chaos, basically, because it lacks structure,” says Xue.
“That makes it one of the holy grails of cancer medication development, together with its direct influence on so many different types of cancer. We can’t believe it’s finally within our reach.”
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References:
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