Scientists succeed in stopping cancer engine fueling 75% of tumors

Scientists have developed a peptide that holds promise in controlling the activity of the MYC protein, a key contributor to exacerbating 75 percent of human cancer cases. According to researchers from the University of California, Riverside, this discovery might pave the way for developing more effective cancer treatments.

The identified peptide compound binds to the shapeless MYC protein and efficiently inhibits its function. As per the release, this protein guides the transcription process in normal cells, converting genetic information from DNA to RNA and, ultimately, into proteins. "Normally, MYC's activity is strictly controlled.

In cancer cells, it becomes hyperactive and is not regulated properly," said Min Xue, a UCR associate professor of chemistry. "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," Xue explained.

Controlling MYC's hyperactivity The study began with the objective of developing a way to reduce MYC's excessive activity. However, controlling the hyperactivity of MYC has proved to be challenging due to its unique characteristics — unlike many other proteins, MYC lacks a definite structure.

"It's basically a glob of randomness. Conventional drug discovery pipelines rely on well defined structures, and this does not exist for MYC," said Xue. After years of dedicated effort, the research team pinpointed a novel peptide that directly binds to MYC. This is referred to as sub micro molar affinity.

This amount of affinity is comparable to that found in antibodies, indicating a highly powerful and specific interaction, as per the study. "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," said Xue in a The research team has been working actively to improve the binding properties of the found peptide to make it appropriate for prospective drug development applications. Presently, they are utilizing lipid nanoparticles as a delivery method for the peptide into cells.

Lipid nanoparticles are small spheres composed of fatty molecules, and although effective for delivery, they may not be optimal as a standalone drug. The researchers are attempting to improve the lead peptide's chemical characteristics to improve its capacity to penetrate cells. The peptide will connect to the MYC protein once within the cell, causing changes in MYC's physical characteristics.

This binding relationship is designed to prevent MYC from performing its normal transcription functions, perhaps providing a tailored way for limiting the protein's activity in cancer cells. The were published on January 3..