Researchers at the University of California-Riverside introduce a groundbreaking method to regulate the MYC protein, a key factor in 75% of human cancer cases. This innovative approach offers renewed optimism in the ongoing fight against cancer, marking a significant development in the New Year.
Traditional drug development approaches unable to target MYC
MYC, an essential shape-shifting protein, plays a critical role in normal cell transcription. It converts genetic information from DNA to RNA for protein synthesis. In cancer cells, MYC becomes hyperactive and uncontrolled, disrupting normal cellular processes.
According to Min Xue, a chemistry associate professor at UC Riverside, the usual regulation of MYC’s activity is disrupted in cancer cells, leading to hyperactivity and uncontrolled growth. Xue explains that MYC acts as a cancer-promoting steroid in 75% of human cancer cases, fueling rapid proliferation.
The challenge in targeting MYC stems from its structure, described as “a glob of randomness,” making traditional drug development strategies ineffective. Conventional drug development strategies often depend on well-develop structures in creating drugs, an approach that is challenging with MYC.
The UC Riverside team achieved a breakthrough by unveiling a peptide compound that effectively binds to MYC, suppressing its hyperactivity. This development, originating from research since 2018, demonstrates that modifying a peptide’s rigidity and shape enhances its interaction with structureless proteins like MYC.
Newly developed peptide has sub-micro-molar affinity
Peptides, in diverse forms, shapes, and positions, gain binding efficiency when bent and connected into rings, limiting their randomness. The newly developed peptide exhibits sub-micro-molar affinity, showcasing specific and potent interactions comparable to antibodies. A remarkable two-order-of-magnitude enhancement in binding performance positions it closer to achieving drug development objectives, marking a significant progress.
The primary emphasis is on transporting a peptide into cells through lipid nanoparticles, small spheres composed of fatty molecules. Though not optimal for drug application, efforts are underway to improve the peptide’s cell penetration capabilities. Once inside a cell, the peptide interacts with MYC, modifying its physical properties and impeding its involvement in transcription activities. This pioneering method holds potential for a groundbreaking approach to cancer treatment, specifically targeting the disruptive nature of MYC.
