The researchers of UC Riverside they made a peptide which binds to MYCa shapeless protein responsible for worsening most cases of cancer. They managed to tame the chaotic proteins, offering hope for a new era of treatments.
In healthy cells, MYC helps drive the transcription process, in which genetic information is converted from DNA into RNA and, finally, into proteins. “Normally, the activity of the MYC protein is tightly controlled. In tumor cells it becomes overactive and is not regulated properly,” he said Min XueUCR associate professor of chemistry.
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Unlike most other proteins, MYC has no structure. “It’s basically a mass of randomness – said Professor Xue -. Conventional drug discovery pipelines rely on well-defined structures, and this doesn’t exist for the MYC protein, which is less like food for cancer cells and more like a steroid that promotes rapid cancer growth. That’s why MYC is responsible for 75% of all human cancer cases.”
A new paper published in the Journal of the American Chemical Society, of which Xue is the senior author, describes a peptide compound that binds to the MYC protein and suppresses its activity. “We have improved the binding performance of this peptide compared to previous versions by two orders of magnitude. This brings it closer to our drug development goals.”
Researchers are developing chemistry that improves the peptide’s ability to penetrate cells.
Full text of the article published on JACS
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